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Protein

Phosphatidate phosphatase LPIN1

Gene

Lpin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays important roles in controlling the metabolism of fatty acids at differents 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.1 Publication

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by N-ethylmaleimide treatment.1 Publication

GO - Molecular functioni

  • histone deacetylase binding Source: MGI
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • phosphatidate phosphatase activity Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: MGI
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: MGI
  • cellular response to insulin stimulus Source: MGI
  • dephosphorylation Source: MGI
  • fat cell differentiation Source: UniProtKB
  • fatty acid catabolic process Source: UniProtKB
  • lipid metabolic process Source: MGI
  • mitochondrial fission Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of histone deacetylation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of fat cell differentiation Source: MGI
  • ruffle organization Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • triglyceride biosynthetic process Source: GO_Central
  • triglyceride mobilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi3.1.3.4. 3474.

Chemistry

SwissLipidsiSLP:000000601.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate phosphatase LPIN1 (EC:3.1.3.4)
Alternative name(s):
Fatty liver dystrophy protein
Lipin-1
Gene namesi
Name:Lpin1
Synonyms:Fld
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1891340. Lpin1.

Subcellular locationi

Isoform 1 :
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.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • mitochondrial outer membrane Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061S → A: Abolishes phosphorylation in response to insulin but has no effect on cellular location. 1 Publication
Mutagenesisi599 – 5991K → R: Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-629. 1 Publication
Mutagenesisi629 – 6291K → R: Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-599. 1 Publication
Mutagenesisi712 – 7121D → A or E: Abolishes phosphatidate phosphatase activity. No effect on interaction or coactivation with PPARA. 2 Publications
Mutagenesisi726 – 7261I → F: Diminishes significantly the interaction and coactivation OF PPARA; when associated with F-727. 1 Publication
Mutagenesisi727 – 7271L → F: Diminishes significantly the interaction and coactivation OF PPARA; when associated with F-726. 1 Publication

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 924924Phosphatidate phosphatase LPIN1PRO_0000209880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei285 – 2851Phosphoserine1 Publication
Modified residuei287 – 2871Phosphoserine1 Publication
Modified residuei293 – 2931Phosphoserine1 Publication
Modified residuei298 – 2981Phosphothreonine1 Publication
Modified residuei328 – 3281PhosphoserineCombined sources1 Publication
Modified residuei392 – 3921Phosphoserine1 Publication
Modified residuei468 – 4681Phosphoserine1 Publication
Modified residuei472 – 4721Phosphoserine1 Publication
Modified residuei483 – 4831Phosphoserine1 Publication
Cross-linki599 – 599Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki629 – 629Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei634 – 6341Phosphoserine1 Publication
Modified residuei635 – 6351Phosphoserine1 Publication
Modified residuei921 – 9211Phosphoserine1 Publication
Modified residuei923 – 9231Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91ZP3.
MaxQBiQ91ZP3.
PaxDbiQ91ZP3.
PRIDEiQ91ZP3.

PTM databases

iPTMnetiQ91ZP3.
PhosphoSiteiQ91ZP3.

Expressioni

Tissue specificityi

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.4 Publications

Inductioni

By fasting, glucocorticoids and diabetes in the liver in a PPARGC1A-dependent manner. Up-regulated during differentiation of 3T3-L1 pre-adipocytes.1 Publication

Gene expression databases

BgeeiQ91ZP3.
CleanExiMM_LPIN1.

Interactioni

Subunit structurei

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.2 Publications

GO - Molecular functioni

  • histone deacetylase binding Source: MGI
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi199700. 1 interaction.
IntActiQ91ZP3. 2 interactions.
MINTiMINT-4610704.
STRINGi10090.ENSMUSP00000070583.

Structurei

3D structure databases

ProteinModelPortaliQ91ZP3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 108108N-LIPAdd
BLAST
Regioni658 – 864207C-LIPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi153 – 1586Nuclear localization signalSequence analysis
Motifi712 – 7165DXDXT motif
Motifi723 – 7275LXXIL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi632 – 6354Poly-Ser

Domaini

Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.
Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional binding motif, which mediates interaction with PPARA.

Sequence similaritiesi

Belongs to the lipin family.Curated

Phylogenomic databases

eggNOGiKOG2116. Eukaryota.
COG5083. LUCA.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ91ZP3.
KOiK15728.
PhylomeDBiQ91ZP3.
TreeFamiTF314095.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR031703. Lipin_mid.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
IPR028794. LPIN1.
[Graphical view]
PANTHERiPTHR12181:SF10. PTHR12181:SF10. 1 hit.
PfamiPF16876. Lipin_mid. 1 hit.
PF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91ZP3-1) [UniParc]FASTAAdd to basket

Also known as: Lipin-beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNYVGQLAGQ VFVTVKELYK GLNPATLSGC IDIIVIRQPN GSLQCSPFHV
60 70 80 90 100
RFGKMGVLRS REKVVDIEIN GESVDLHMKL GDNGEAFFVQ ETDNDQEIIP
110 120 130 140 150
MYLATSPILS EGAARMESQL KRNSVDRIRC LDPTTAAQGL PPSDTPSTGS
160 170 180 190 200
LGKKRRKRRR KAQLDNLKRD DNVNSSEDED MFPIEMSSDE DTAPMDGSRT
210 220 230 240 250
LPNDVPPFQD DIPKENFPSI STHPQSASYP SSDREWSPSP SSLVDCQRTP
260 270 280 290 300
PHLAEGVLSS SCPLQSCHFH ASESPSGSRP STPKSDSELV SKSADRLTPK
310 320 330 340 350
NNLEMLWLWG ELPQAAKSSS PHKMKESSPL GSRKTPDKMN FQAIHSESSD
360 370 380 390 400
TFSDQSPTMA RGLLIHQSKA QTEMQFVNEE DLESLGAAAP PSPVAEELKA
410 420 430 440 450
PYPNTAQSSS KTDSPSRKKD KRSRHLGADG VYLDDLTDMD PEVAALYFPK
460 470 480 490 500
NGDPGGLPKQ ASDNGARSAN QSPQSVGGSG IDSGVESTSD SLRDLPSIAI
510 520 530 540 550
SLCGGLSDHR EITKDAFLEQ AVSYQQFADN PAIIDDPNLV VKVGNKYYNW
560 570 580 590 600
TTAAPLLLAM QAFQKPLPKA TVESIMRDKM PKKGGRWWFS WRGRNATIKE
610 620 630 640 650
ESKPEQCLTG KGHNTGEQPA QLGLATRIKH ESSSSDEEHA AAKPSGSSHL
660 670 680 690 700
SLLSNVSYKK TLRLTSEQLK SLKLKNGPND VVFSVTTQYQ GTCRCEGTIY
710 720 730 740 750
LWNWDDKVII SDIDGTITRS DTLGHILPTL GKDWTHQGIA KLYHKVSQNG
760 770 780 790 800
YKFLYCSARA IGMADMTRGY LHWVNERGTV LPQGPLLLSP SSLFSALHRE
810 820 830 840 850
VIEKKPEKFK VQCLTDIKNL FFPNTEPFYA AFGNRPADVY SYKQVGVSLN
860 870 880 890 900
RIFTVNPKGE LVQEHAKTNI SSYVRLCEVV DHVFPLLKRS HSCDFPCSDT
910 920
FSNFTFWREP LPPFENQDMH SASA
Length:924
Mass (Da):102,002
Last modified:December 1, 2001 - v1
Checksum:i175F90E9159A216A
GO
Isoform 2 (identifier: Q91ZP3-2) [UniParc]FASTAAdd to basket

Also known as: Lipin-alpha

The sequence of this isoform differs from the canonical sequence as follows:
     241-273: Missing.

Note: Mutagenesis of 724:Ser->Leu abolishes phosphatidate phosphatase activity but does not prevent membrane association.
Show »
Length:891
Mass (Da):98,496
Checksum:i52303A406C235957
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751S → T in BAB31786 (PubMed:16141072).Curated
Sequence conflicti175 – 1751S → T in BAB29412 (PubMed:16141072).Curated
Sequence conflicti223 – 2231H → Y in BAB31786 (PubMed:16141072).Curated
Sequence conflicti223 – 2231H → Y in BAB29412 (PubMed:16141072).Curated
Sequence conflicti465 – 4651G → V in AAF44296 (PubMed:11138012).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841G → R in allele FLD2J. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei241 – 27333Missing in isoform 2. 1 PublicationVSP_003134Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF412811 mRNA. Translation: AAL07798.1.
AF180471 mRNA. Translation: AAF44296.1.
AK019539 mRNA. Translation: BAB31786.1.
AK014526 mRNA. Translation: BAB29412.1.
CCDSiCCDS25822.1. [Q91ZP3-1]
CCDS25823.1. [Q91ZP3-2]
RefSeqiNP_001123884.1. NM_001130412.1.
NP_056578.2. NM_015763.4.
NP_766538.2. NM_172950.3.
XP_006515051.1. XM_006514988.2.
UniGeneiMm.153625.

Genome annotation databases

GeneIDi14245.
KEGGimmu:14245.
UCSCiuc007nbs.2. mouse. [Q91ZP3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF412811 mRNA. Translation: AAL07798.1.
AF180471 mRNA. Translation: AAF44296.1.
AK019539 mRNA. Translation: BAB31786.1.
AK014526 mRNA. Translation: BAB29412.1.
CCDSiCCDS25822.1. [Q91ZP3-1]
CCDS25823.1. [Q91ZP3-2]
RefSeqiNP_001123884.1. NM_001130412.1.
NP_056578.2. NM_015763.4.
NP_766538.2. NM_172950.3.
XP_006515051.1. XM_006514988.2.
UniGeneiMm.153625.

3D structure databases

ProteinModelPortaliQ91ZP3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199700. 1 interaction.
IntActiQ91ZP3. 2 interactions.
MINTiMINT-4610704.
STRINGi10090.ENSMUSP00000070583.

Chemistry

SwissLipidsiSLP:000000601.

PTM databases

iPTMnetiQ91ZP3.
PhosphoSiteiQ91ZP3.

Proteomic databases

EPDiQ91ZP3.
MaxQBiQ91ZP3.
PaxDbiQ91ZP3.
PRIDEiQ91ZP3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14245.
KEGGimmu:14245.
UCSCiuc007nbs.2. mouse. [Q91ZP3-1]

Organism-specific databases

CTDi23175.
MGIiMGI:1891340. Lpin1.

Phylogenomic databases

eggNOGiKOG2116. Eukaryota.
COG5083. LUCA.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ91ZP3.
KOiK15728.
PhylomeDBiQ91ZP3.
TreeFamiTF314095.

Enzyme and pathway databases

BRENDAi3.1.3.4. 3474.

Miscellaneous databases

ChiTaRSiLpin1. mouse.
PROiQ91ZP3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZP3.
CleanExiMM_LPIN1.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR031703. Lipin_mid.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
IPR028794. LPIN1.
[Graphical view]
PANTHERiPTHR12181:SF10. PTHR12181:SF10. 1 hit.
PfamiPF16876. Lipin_mid. 1 hit.
PF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin."
    Huffman T.A., Mothe-Satney I., Lawrence J.C. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 99:1047-1052(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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.
  2. "Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin."
    Peterfy M., Phan J., Xu P., Reue K.
    Nat. Genet. 27:121-124(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, VARIANT FLD2J ARG-84.
    Strain: BALB/cJ.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Skin and Testis.
  4. "Alternatively spliced lipin isoforms exhibit distinct expression pattern, subcellular localization, and role in adipogenesis."
    Peterfy M., Phan J., Reue K.
    J. Biol. Chem. 280:32883-32889(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha regulatory pathway."
    Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E., Lawrence J.C. Jr., Kelly D.P.
    Cell Metab. 4:199-210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS COACTIVATOR, MUTAGENESIS OF ASP-712; ILE-726 AND LEU-727, INDUCTION, INTERACTION WITH PPARGC1A AND PPARA.
  6. "Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1."
    Harris T.E., Huffman T.A., Chi A., Shabanowitz J., Hunt D.F., Kumar A., Lawrence J.C. Jr.
    J. Biol. Chem. 282:277-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns."
    Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.
    J. Biol. Chem. 282:3450-3457(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, COFACTOR, ENZYME REGULATION.
  8. "A conserved serine residue is required for the phosphatidate phosphatase activity but not the transcriptional coactivator functions of lipin-1 and lipin-2."
    Donkor J., Zhang P., Wong S., O'Loughlin L., Dewald J., Kok B.P., Brindley D.N., Reue K.
    J. Biol. Chem. 284:29968-29978(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF SER-106.
  9. "Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells."
    Liu G.H., Gerace L.
    PLoS ONE 4:E7031-E7031(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-599 AND LYS-629, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-599 AND LYS-629, TISSUE SPECIFICITY, INTERACTION WITH MEF2C.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Testis.
  11. "piRNA-associated germline nuage formation and spermatogenesis require MitoPLD profusogenic mitochondrial-surface lipid signaling."
    Huang H., Gao Q., Peng X., Choi S.Y., Sarma K., Ren H., Morris A.J., Frohman M.A.
    Dev. Cell 20:376-387(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), MUTAGENESIS OF ASP-712.
  12. "Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is the metazoan SPO7 ortholog and functions in the lipin activation pathway."
    Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R., Graham M., Reue K., Dixon J.E., Goodman J.M.
    J. Biol. Chem. 287:3123-3137(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY CTDNEP1.

Entry informationi

Entry nameiLPIN1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZP3
Secondary accession number(s): Q9CQI2, Q9JLG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.