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Protein

Phosphatidate phosphatase LPIN1

Gene

LPIN1

Organism
Homo sapiens (Human)
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 in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A/PPARA to modulate lipid metabolism gene expression (By similarity). Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Mg2+ and, at a lesser extent, Mn2+.1 Publication

Enzyme regulationi

Potently inhibited by sphingolipids, in particular, the sphingoid bases sphinganine and sphingosine and ceramide-1-phosphate. Inhibited by concentrations of Mg2+ and Mn2+ above their optimums and by Ca2+, Zn2+, N-ethylmaleimide and propranolol.1 Publication

Kineticsi

  1. KM=0.35 mM for phosphatidate (isoform 1)
  2. KM=0.24 mM for phosphatidate (isoform 3)
  3. KM=0.11 mM for phosphatidate (isoform 4)

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius. Thermolabile above 40 degrees Celsius and essentially inactive at 60 degrees Celsius.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transcription, Transcription regulation

    Enzyme and pathway databases

    BRENDAi3.1.3.4. 2681.
    ReactomeiR-HSA-1483191. Synthesis of PC.
    R-HSA-1483213. Synthesis of PE.
    R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
    R-HSA-75109. Triglyceride Biosynthesis.

    Chemistry

    SwissLipidsiSLP:000000881. [Q14693-1]
    SLP:000000882. [Q14693-3]
    SLP:000000883. [Q14693-4]

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidate phosphatase LPIN1 (EC:3.1.3.4)
    Alternative name(s):
    Lipin-1
    Gene namesi
    Name:LPIN1
    Synonyms:KIAA0188
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:13345. LPIN1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Myoglobinuria, acute recurrent, autosomal recessive (ARARM)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionRecurrent 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.
    See also OMIM:268200

    Organism-specific databases

    MalaCardsiLPIN1.
    MIMi268200. phenotype.
    Orphaneti99845. Genetic recurrent myoglobinuria.
    PharmGKBiPA30436.

    Polymorphism and mutation databases

    BioMutaiLPIN1.
    DMDMi23831266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 890890Phosphatidate phosphatase LPIN1PRO_0000209879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei106 – 1061PhosphoserineBy similarity
    Modified residuei150 – 1501PhosphoserineBy similarity
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei254 – 2541PhosphoserineBy similarity
    Modified residuei260 – 2601PhosphoserineBy similarity
    Modified residuei264 – 2641PhosphothreonineBy similarity
    Modified residuei294 – 2941PhosphoserineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei438 – 4381PhosphoserineBy similarity
    Modified residuei449 – 4491PhosphoserineBy similarity
    Cross-linki565 – 565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki595 – 595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei600 – 6001PhosphoserineBy similarity
    Modified residuei601 – 6011PhosphoserineBy similarity
    Modified residuei887 – 8871PhosphoserineBy similarity
    Modified residuei889 – 8891PhosphoserineBy similarity

    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 (By similarity).By similarity
    Sumoylated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiQ14693.
    MaxQBiQ14693.
    PaxDbiQ14693.
    PRIDEiQ14693.

    PTM databases

    DEPODiQ14693.
    iPTMnetiQ14693.
    PhosphoSiteiQ14693.

    Expressioni

    Tissue specificityi

    Specifically expressed in skeletal muscle. Also abundant in adipose tissue. Lower levels in some portions of the digestive tract.2 Publications

    Gene expression databases

    BgeeiQ14693.
    CleanExiHS_LPIN1.
    ExpressionAtlasiQ14693. baseline and differential.
    GenevisibleiQ14693. HS.

    Organism-specific databases

    HPAiHPA038021.

    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.By similarity

    Protein-protein interaction databases

    BioGridi116787. 9 interactions.
    IntActiQ14693. 3 interactions.
    STRINGi9606.ENSP00000256720.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14693.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 108108N-LIPAdd
    BLAST
    Regioni624 – 830207C-LIPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi153 – 1586Nuclear localization signalSequence analysis
    Motifi678 – 6825DXDXT motif
    Motifi689 – 6935LXXIL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi147 – 1504Poly-Ser
    Compositional biasi598 – 6014Poly-Ser

    Domaini

    Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional binding motif, which mediates interaction with PPARA.By similarity

    Sequence similaritiesi

    Belongs to the lipin family.Curated

    Phylogenomic databases

    eggNOGiKOG2116. Eukaryota.
    COG5083. LUCA.
    GeneTreeiENSGT00390000011286.
    HOGENOMiHOG000202965.
    HOVERGENiHBG052338.
    InParanoidiQ14693.
    KOiK15728.
    OMAiNVQTMNY.
    OrthoDBiEOG7QZG8X.
    PhylomeDBiQ14693.
    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 (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q14693-1) [UniParc]FASTAAdd to basket

    Also known as: Alpha

    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 GNLQCSPFHV
    60 70 80 90 100
    RFGKMGVLRS REKVVDIEIN GESVDLHMKL GDNGEAFFVQ ETDNDQEVIP
    110 120 130 140 150
    MHLATSPILS EGASRMECQL KRGSVDRMRG LDPSTPAQVI APSETPSSSS
    160 170 180 190 200
    VVKKRRKRRR KSQLDSLKRD DNMNTSEDED MFPIEMSSDE AMELLESSRT
    210 220 230 240 250
    LPNDIPPFQD DIPEENLSLA VIYPQSASYP NSDREWSPTP SPSGSRPSTP
    260 270 280 290 300
    KSDSELVSKS TERTGQKNPE MLWLWGELPQ AAKSSSPHKM KESSPLSSRK
    310 320 330 340 350
    ICDKSHFQAI HSESSDTFSD QSPTLVGGAL LDQNKPQTEM QFVNEEDLET
    360 370 380 390 400
    LGAAAPLLPM IEELKPPSAS VVQTANKTDS PSRKRDKRSR HLGADGVYLD
    410 420 430 440 450
    DLTDMDPEVA ALYFPKNGDP SGLAKHASDN GARSANQSPQ SVGSSGVDSG
    460 470 480 490 500
    VESTSDGLRD LPSIAISLCG GLSDHREITK DAFLEQAVSY QQFVDNPAII
    510 520 530 540 550
    DDPNLVVKIG SKYYNWTTAA PLLLAMQAFQ KPLPKATVES IMRDKMPKKG
    560 570 580 590 600
    GRWWFSWRGR NTTIKEESKP EQCLAGKAHS TGEQPPQLSL ATRVKHESSS
    610 620 630 640 650
    SDEERAAAKP SNAGHLPLLP NVSYKKTLRL TSEQLKSLKL KNGPNDVVFS
    660 670 680 690 700
    VTTQYQGTCR CEGTIYLWNW DDKVIISDID GTITRSDTLG HILPTLGKDW
    710 720 730 740 750
    THQGIAKLYH KVSQNGYKFL YCSARAIGMA DMTRGYLHWV NERGTVLPQG
    760 770 780 790 800
    PLLLSPSSLF SALHREVIEK KPEKFKVQCL TDIKNLFFPN TEPFYAAFGN
    810 820 830 840 850
    RPADVYSYKQ VGVSLNRIFT VNPKGELVQE HAKTNISSYV RLCEVVDHVF
    860 870 880 890
    PLLKRSHSSD FPCSDTFSNF TFWREPLPPF ENQDIHSASA
    Length:890
    Mass (Da):98,664
    Last modified:October 10, 2002 - v2
    Checksum:i781761FC47E9CEE7
    GO
    Isoform 2 (identifier: Q14693-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSRVQTM

    Note: No experimental confirmation available.
    Show »
    Length:896
    Mass (Da):99,367
    Checksum:iCBE905D33C8D62CD
    GO
    Isoform 3 (identifier: Q14693-3) [UniParc]FASTAAdd to basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         241-241: S → SSLVDCKRTAPHLAVAAEGGLSSSCPPQSSLFHPSES

    Show »
    Length:926
    Mass (Da):102,313
    Checksum:i3CAB6B85233F6AAD
    GO
    Isoform 4 (identifier: Q14693-4) [UniParc]FASTAAdd to basket

    Also known as: Gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         535-535: K → KSSCLSYLHVILDAIRFCFSKIFNAQI

    Show »
    Length:916
    Mass (Da):101,636
    Checksum:iA1594A83FE86D930
    GO
    Isoform 5 (identifier: Q14693-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSRVQTM
         241-241: S → SSLVDCKRTAPHLAVAAEGGLSSSCPPQSSLFHPSES

    Note: No experimental confirmation available.
    Show »
    Length:932
    Mass (Da):103,016
    Checksum:iDC45B264870384D8
    GO
    Isoform 6 (identifier: Q14693-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSRVQTM
         241-241: S → SSLVDCKRTAPHLAVAAEGGLSSSCPPQSSLFHPSES
         417-417: N → K
         418-890: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:459
    Mass (Da):50,528
    Checksum:iDC0514AD1A5C4922
    GO
    Isoform 7 (identifier: Q14693-7) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGEQDGIRSSSWETSQGKSSPDSAWSWIPIMRDPGWIRNVWSSNINVQTM
         241-241: S → SSLVDCKRTAPHLAVAAEGGLSSSCPPQSSLFHPSES

    Note: No experimental confirmation available.
    Show »
    Length:975
    Mass (Da):107,861
    Checksum:iFE3F7C4BBA831395
    GO

    Sequence cautioni

    The sequence BAA11505.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAG57200.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAG57885.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAG57957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BC018071 differs from that shown. Reason: Frameshift at position 134. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711D → G in BC018071 (PubMed:15489334).Curated
    Sequence conflicti210 – 2101D → G in BAG57885 (PubMed:14702039).Curated
    Sequence conflicti316 – 3161D → Y in BAH13844 (PubMed:14702039).Curated
    Sequence conflicti535 – 5351K → R in BAH13844 (PubMed:14702039).Curated
    Sequence conflicti592 – 5921T → I in BAG57885 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561G → E in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035874
    Natural varianti610 – 6101P → S.1 Publication
    Corresponds to variant rs4669781 [ dbSNP | Ensembl ].
    VAR_013885
    Natural varianti637 – 6371S → T.1 Publication
    Corresponds to variant rs17852755 [ dbSNP | Ensembl ].
    VAR_054878

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSRVQTM in isoform 2, isoform 5 and isoform 6. 2 PublicationsVSP_045533
    Alternative sequencei1 – 11M → MGEQDGIRSSSWETSQGKSS PDSAWSWIPIMRDPGWIRNV WSSNINVQTM in isoform 7. CuratedVSP_055384
    Alternative sequencei241 – 2411S → SSLVDCKRTAPHLAVAAEGG LSSSCPPQSSLFHPSES in isoform 3, isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_053970
    Alternative sequencei417 – 4171N → K in isoform 6. 1 PublicationVSP_055361
    Alternative sequencei418 – 890473Missing in isoform 6. 1 PublicationVSP_055362Add
    BLAST
    Alternative sequencei535 – 5351K → KSSCLSYLHVILDAIRFCFS KIFNAQI in isoform 4. 1 PublicationVSP_053971

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D80010 mRNA. Translation: BAA11505.1. Different initiation.
    AK290235 mRNA. Translation: BAF82924.1.
    AK293787 mRNA. Translation: BAG57200.1. Different initiation.
    AK294742 mRNA. Translation: BAG57885.1. Different initiation.
    AK294853 mRNA. Translation: BAG57957.1. Different initiation.
    AK302922 mRNA. Translation: BAH13844.1.
    AC012456 Genomic DNA. Translation: AAY14695.1.
    AC106875 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00918.1.
    CH471053 Genomic DNA. Translation: EAX00920.1.
    BC018071 mRNA. No translation available.
    BC030537 mRNA. Translation: AAH30537.1.
    CCDSiCCDS1682.1. [Q14693-1]
    CCDS58699.1. [Q14693-7]
    CCDS58700.1. [Q14693-6]
    CCDS58701.1. [Q14693-2]
    RefSeqiNP_001248356.1. NM_001261427.1. [Q14693-2]
    NP_001248357.1. NM_001261428.1. [Q14693-7]
    NP_001248358.1. NM_001261429.1. [Q14693-6]
    NP_663731.1. NM_145693.2. [Q14693-1]
    XP_006711933.1. XM_006711870.2. [Q14693-5]
    XP_006711934.1. XM_006711871.1. [Q14693-3]
    XP_006711935.1. XM_006711872.1. [Q14693-3]
    XP_006711937.1. XM_006711874.1. [Q14693-3]
    XP_011508636.1. XM_011510334.1. [Q14693-5]
    XP_011508637.1. XM_011510335.1. [Q14693-3]
    XP_011508638.1. XM_011510336.1. [Q14693-3]
    UniGeneiHs.467740.
    Hs.739141.

    Genome annotation databases

    EnsembliENST00000256720; ENSP00000256720; ENSG00000134324. [Q14693-1]
    ENST00000396097; ENSP00000379404; ENSG00000134324. [Q14693-5]
    ENST00000396098; ENSP00000379405; ENSG00000134324. [Q14693-6]
    ENST00000425416; ENSP00000401522; ENSG00000134324. [Q14693-2]
    ENST00000449576; ENSP00000397908; ENSG00000134324. [Q14693-7]
    GeneIDi23175.
    KEGGihsa:23175.
    UCSCiuc002rbs.5. human. [Q14693-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D80010 mRNA. Translation: BAA11505.1. Different initiation.
    AK290235 mRNA. Translation: BAF82924.1.
    AK293787 mRNA. Translation: BAG57200.1. Different initiation.
    AK294742 mRNA. Translation: BAG57885.1. Different initiation.
    AK294853 mRNA. Translation: BAG57957.1. Different initiation.
    AK302922 mRNA. Translation: BAH13844.1.
    AC012456 Genomic DNA. Translation: AAY14695.1.
    AC106875 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00918.1.
    CH471053 Genomic DNA. Translation: EAX00920.1.
    BC018071 mRNA. No translation available.
    BC030537 mRNA. Translation: AAH30537.1.
    CCDSiCCDS1682.1. [Q14693-1]
    CCDS58699.1. [Q14693-7]
    CCDS58700.1. [Q14693-6]
    CCDS58701.1. [Q14693-2]
    RefSeqiNP_001248356.1. NM_001261427.1. [Q14693-2]
    NP_001248357.1. NM_001261428.1. [Q14693-7]
    NP_001248358.1. NM_001261429.1. [Q14693-6]
    NP_663731.1. NM_145693.2. [Q14693-1]
    XP_006711933.1. XM_006711870.2. [Q14693-5]
    XP_006711934.1. XM_006711871.1. [Q14693-3]
    XP_006711935.1. XM_006711872.1. [Q14693-3]
    XP_006711937.1. XM_006711874.1. [Q14693-3]
    XP_011508636.1. XM_011510334.1. [Q14693-5]
    XP_011508637.1. XM_011510335.1. [Q14693-3]
    XP_011508638.1. XM_011510336.1. [Q14693-3]
    UniGeneiHs.467740.
    Hs.739141.

    3D structure databases

    ProteinModelPortaliQ14693.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116787. 9 interactions.
    IntActiQ14693. 3 interactions.
    STRINGi9606.ENSP00000256720.

    Chemistry

    SwissLipidsiSLP:000000881. [Q14693-1]
    SLP:000000882. [Q14693-3]
    SLP:000000883. [Q14693-4]

    PTM databases

    DEPODiQ14693.
    iPTMnetiQ14693.
    PhosphoSiteiQ14693.

    Polymorphism and mutation databases

    BioMutaiLPIN1.
    DMDMi23831266.

    Proteomic databases

    EPDiQ14693.
    MaxQBiQ14693.
    PaxDbiQ14693.
    PRIDEiQ14693.

    Protocols and materials databases

    DNASUi23175.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000256720; ENSP00000256720; ENSG00000134324. [Q14693-1]
    ENST00000396097; ENSP00000379404; ENSG00000134324. [Q14693-5]
    ENST00000396098; ENSP00000379405; ENSG00000134324. [Q14693-6]
    ENST00000425416; ENSP00000401522; ENSG00000134324. [Q14693-2]
    ENST00000449576; ENSP00000397908; ENSG00000134324. [Q14693-7]
    GeneIDi23175.
    KEGGihsa:23175.
    UCSCiuc002rbs.5. human. [Q14693-1]

    Organism-specific databases

    CTDi23175.
    GeneCardsiLPIN1.
    HGNCiHGNC:13345. LPIN1.
    HPAiHPA038021.
    MalaCardsiLPIN1.
    MIMi268200. phenotype.
    605518. gene.
    neXtProtiNX_Q14693.
    Orphaneti99845. Genetic recurrent myoglobinuria.
    PharmGKBiPA30436.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2116. Eukaryota.
    COG5083. LUCA.
    GeneTreeiENSGT00390000011286.
    HOGENOMiHOG000202965.
    HOVERGENiHBG052338.
    InParanoidiQ14693.
    KOiK15728.
    OMAiNVQTMNY.
    OrthoDBiEOG7QZG8X.
    PhylomeDBiQ14693.
    TreeFamiTF314095.

    Enzyme and pathway databases

    BRENDAi3.1.3.4. 2681.
    ReactomeiR-HSA-1483191. Synthesis of PC.
    R-HSA-1483213. Synthesis of PE.
    R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
    R-HSA-75109. Triglyceride Biosynthesis.

    Miscellaneous databases

    ChiTaRSiLPIN1. human.
    GeneWikiiLPIN1.
    GenomeRNAii23175.
    PROiQ14693.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ14693.
    CleanExiHS_LPIN1.
    ExpressionAtlasiQ14693. baseline and differential.
    GenevisibleiQ14693. HS.

    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. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 481-890 (ISOFORM 3).
      Tissue: Brain, Cerebellum, Testis and Thalamus.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), VARIANT THR-637.
      Tissue: Hippocampus and Uterus.
    6. "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: TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms."
      Han G.S., Carman G.M.
      J. Biol. Chem. 285:14628-14638(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1; 3 AND 4), ENZYME REGULATION, COFACTOR.
    10. "Identification of single-nucleotide polymorphisms in the human LPIN1 gene."
      Cao H., Hegele R.A.
      J. Hum. Genet. 47:370-372(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-610.
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-56.
    12. Cited for: INVOLVEMENT IN ARARM.
    13. "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.

    Entry informationi

    Entry nameiLPIN1_HUMAN
    AccessioniPrimary (citable) accession number: Q14693
    Secondary accession number(s): A8MU38
    , B4DET9, B4DGS4, B4DGZ6, B5MC18, B7Z858, D6W506, E7ESE7, F5GY24, Q53T25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 10, 2002
    Last modified: June 8, 2016
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    May represent a candidate gene for human lipodysytropy syndromes.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. 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.