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P11150

- LIPC_HUMAN

UniProt

P11150 - LIPC_HUMAN

Protein

Hepatic triacylglycerol lipase

Gene

LIPC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin.

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681NucleophileBy similarity
    Active sitei194 – 1941Charge relay systemPROSITE-ProRule annotation
    Active sitei279 – 2791Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. heparin binding Source: UniProtKB-KW
    3. low-density lipoprotein particle binding Source: BHF-UCL
    4. phospholipase activity Source: BHF-UCL
    5. triglyceride lipase activity Source: BHF-UCL

    GO - Biological processi

    1. cholesterol homeostasis Source: BHF-UCL
    2. cholesterol metabolic process Source: Ensembl
    3. chylomicron remnant clearance Source: BHF-UCL
    4. fatty acid biosynthetic process Source: BHF-UCL
    5. high-density lipoprotein particle remodeling Source: BHF-UCL
    6. intermediate-density lipoprotein particle remodeling Source: BHF-UCL
    7. low-density lipoprotein particle remodeling Source: BHF-UCL
    8. phosphatidylcholine catabolic process Source: BHF-UCL
    9. reverse cholesterol transport Source: BHF-UCL
    10. triglyceride catabolic process Source: BHF-UCL
    11. triglyceride homeostasis Source: BHF-UCL
    12. very-low-density lipoprotein particle remodeling Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hepatic triacylglycerol lipase (EC:3.1.1.3)
    Short name:
    HL
    Short name:
    Hepatic lipase
    Alternative name(s):
    Lipase member C
    Gene namesi
    Name:LIPC
    Synonyms:HTGL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6619. LIPC.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: BHF-UCL
    2. high-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    HDL, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Hepatic lipase deficiency (HL deficiency) [MIM:614025]: A disorder characterized by elevated levels of beta-migrating very low density lipoproteins, and abnormally triglyceride-rich low and high density lipoproteins.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti134 – 1341V → VHYTVAV in HL deficiency. 1 Publication
    VAR_004207
    Natural varianti289 – 2891S → F in HL deficiency. 2 Publications
    Corresponds to variant rs121912502 [ dbSNP | Ensembl ].
    VAR_004209
    Natural varianti405 – 4051T → M in HL deficiency. 2 Publications
    Corresponds to variant rs28933094 [ dbSNP | Ensembl ].
    VAR_004210

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi125853. phenotype.
    612797. phenotype.
    614025. phenotype.
    Orphaneti140905. Hyperlipidemia due to hepatic triglyceride lipase deficiency.
    PharmGKBiPA230.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 499477Hepatic triacylglycerol lipasePRO_0000017769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP11150.
    PRIDEiP11150.

    PTM databases

    PhosphoSiteiP11150.

    Expressioni

    Gene expression databases

    ArrayExpressiP11150.
    BgeeiP11150.
    CleanExiHS_LIPC.
    GenevestigatoriP11150.

    Organism-specific databases

    HPAiCAB016141.

    Interactioni

    Protein-protein interaction databases

    BioGridi110178. 4 interactions.
    IntActiP11150. 1 interaction.
    STRINGi9606.ENSP00000299022.

    Structurei

    3D structure databases

    ProteinModelPortaliP11150.
    SMRiP11150. Positions 47-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini352 – 486135PLATPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni181 – 19313Heparin-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG81747.
    HOGENOMiHOG000038553.
    HOVERGENiHBG002259.
    InParanoidiP11150.
    KOiK01046.
    OrthoDBiEOG757CX5.
    PhylomeDBiP11150.
    TreeFamiTF324997.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR002333. Lipase_hep.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PTHR11610:SF2. PTHR11610:SF2. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00824. HEPLIPASE.
    PR00821. TAGLIPASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11150-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTSPLCFSI LLVLCIFIQS SALGQSLKPE PFGRRAQAVE TNKTLHEMKT    50
    RFLLFGETNQ GCQIRINHPD TLQECGFNSS LPLVMIIHGW SVDGVLENWI 100
    WQMVAALKSQ PAQPVNVGLV DWITLAHDHY TIAVRNTRLV GKEVAALLRW 150
    LEESVQLSRS HVHLIGYSLG AHVSGFAGSS IGGTHKIGRI TGLDAAGPLF 200
    EGSAPSNRLS PDDANFVDAI HTFTREHMGL SVGIKQPIGH YDFYPNGGSF 250
    QPGCHFLELY RHIAQHGFNA ITQTIKCSHE RSVHLFIDSL LHAGTQSMAY 300
    PCGDMNSFSQ GLCLSCKKGR CNTLGYHVRQ EPRSKSKRLF LVTRAQSPFK 350
    VYHYQFKIQF INQTETPIQT TFTMSLLGTK EKMQKIPITL GKGIASNKTY 400
    SFLITLDVDI GELIMIKFKW ENSAVWANVW DTVQTIIPWS TGPRHSGLVL 450
    KTIRVKAGET QQRMTFCSEN TDDLLLRPTQ EKIFVKCEIK SKTSKRKIR 499
    Length:499
    Mass (Da):55,914
    Last modified:January 11, 2011 - v3
    Checksum:i1FC7567CAE3E514B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561F → S in AAA61165. (PubMed:2828141)Curated

    Polymorphismi

    Genetic variations in LIPC define the high density lipoprotein cholesterol level quantitative trait locus 12 (HDLCQ12) [MIMi:612797].
    Genetic variations in LIPC are associated with non-insulin-dependent diabetes mellitus susceptibility (NIDDM susceptibility) [MIMi:125853].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951V → M.2 Publications
    Corresponds to variant rs6078 [ dbSNP | Ensembl ].
    VAR_004206
    Natural varianti134 – 1341V → VHYTVAV in HL deficiency. 1 Publication
    VAR_004207
    Natural varianti215 – 2151N → S.6 Publications
    Corresponds to variant rs6083 [ dbSNP | Ensembl ].
    VAR_004208
    Natural varianti289 – 2891S → F in HL deficiency. 2 Publications
    Corresponds to variant rs121912502 [ dbSNP | Ensembl ].
    VAR_004209
    Natural varianti342 – 3421V → I.1 Publication
    Corresponds to variant rs145811475 [ dbSNP | Ensembl ].
    VAR_017024
    Natural varianti356 – 3561F → L.8 Publications
    Corresponds to variant rs3829462 [ dbSNP | Ensembl ].
    VAR_017025
    Natural varianti405 – 4051T → M in HL deficiency. 2 Publications
    Corresponds to variant rs28933094 [ dbSNP | Ensembl ].
    VAR_004210
    Natural varianti409 – 4091D → A.1 Publication
    Corresponds to variant rs142036980 [ dbSNP | Ensembl ].
    VAR_017026
    Natural varianti440 – 4401S → N.1 Publication
    Corresponds to variant rs6079 [ dbSNP | Ensembl ].
    VAR_014179

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83548 mRNA. Translation: BAA12014.1.
    X07228 mRNA. Translation: CAA30188.1.
    J03540 mRNA. Translation: AAA59520.1.
    J03895 mRNA. Translation: AAA61165.1.
    M29194
    , M29186, M29187, M29188, M29189, M29190, M29191, M29192, M29193 Genomic DNA. Translation: AAB60702.1.
    D83062 Genomic DNA. Translation: BAA11760.1.
    M35433
    , M35425, M35426, M35427, M35429, M35430, M35431, M35432 Genomic DNA. Translation: AAA59521.1.
    AK292631 mRNA. Translation: BAF85320.1.
    AK315306 mRNA. Translation: BAG37710.1.
    AC018904 Genomic DNA. No translation available.
    AC084781 Genomic DNA. No translation available.
    BC132825 mRNA. Translation: AAI32826.1.
    BC136495 mRNA. Translation: AAI36496.1.
    AF037404 Genomic DNA. Translation: AAC34206.1.
    CCDSiCCDS10166.1.
    PIRiA28997.
    RefSeqiNP_000227.2. NM_000236.2.
    XP_005254429.1. XM_005254372.1.
    XP_006720564.1. XM_006720501.1.
    UniGeneiHs.654472.

    Genome annotation databases

    EnsembliENST00000299022; ENSP00000299022; ENSG00000166035.
    ENST00000356113; ENSP00000348425; ENSG00000166035.
    GeneIDi3990.
    KEGGihsa:3990.
    UCSCiuc002afa.2. human.

    Polymorphism databases

    DMDMi317373430.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83548 mRNA. Translation: BAA12014.1 .
    X07228 mRNA. Translation: CAA30188.1 .
    J03540 mRNA. Translation: AAA59520.1 .
    J03895 mRNA. Translation: AAA61165.1 .
    M29194
    , M29186 , M29187 , M29188 , M29189 , M29190 , M29191 , M29192 , M29193 Genomic DNA. Translation: AAB60702.1 .
    D83062 Genomic DNA. Translation: BAA11760.1 .
    M35433
    , M35425 , M35426 , M35427 , M35429 , M35430 , M35431 , M35432 Genomic DNA. Translation: AAA59521.1 .
    AK292631 mRNA. Translation: BAF85320.1 .
    AK315306 mRNA. Translation: BAG37710.1 .
    AC018904 Genomic DNA. No translation available.
    AC084781 Genomic DNA. No translation available.
    BC132825 mRNA. Translation: AAI32826.1 .
    BC136495 mRNA. Translation: AAI36496.1 .
    AF037404 Genomic DNA. Translation: AAC34206.1 .
    CCDSi CCDS10166.1.
    PIRi A28997.
    RefSeqi NP_000227.2. NM_000236.2.
    XP_005254429.1. XM_005254372.1.
    XP_006720564.1. XM_006720501.1.
    UniGenei Hs.654472.

    3D structure databases

    ProteinModelPortali P11150.
    SMRi P11150. Positions 47-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110178. 4 interactions.
    IntActi P11150. 1 interaction.
    STRINGi 9606.ENSP00000299022.

    Chemistry

    BindingDBi P11150.
    ChEMBLi CHEMBL2127.

    PTM databases

    PhosphoSitei P11150.

    Polymorphism databases

    DMDMi 317373430.

    Proteomic databases

    PaxDbi P11150.
    PRIDEi P11150.

    Protocols and materials databases

    DNASUi 3990.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299022 ; ENSP00000299022 ; ENSG00000166035 .
    ENST00000356113 ; ENSP00000348425 ; ENSG00000166035 .
    GeneIDi 3990.
    KEGGi hsa:3990.
    UCSCi uc002afa.2. human.

    Organism-specific databases

    CTDi 3990.
    GeneCardsi GC15P058702.
    H-InvDB HIX0038150.
    HGNCi HGNC:6619. LIPC.
    HPAi CAB016141.
    MIMi 125853. phenotype.
    151670. gene.
    612797. phenotype.
    614025. phenotype.
    neXtProti NX_P11150.
    Orphaneti 140905. Hyperlipidemia due to hepatic triglyceride lipase deficiency.
    PharmGKBi PA230.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81747.
    HOGENOMi HOG000038553.
    HOVERGENi HBG002259.
    InParanoidi P11150.
    KOi K01046.
    OrthoDBi EOG757CX5.
    PhylomeDBi P11150.
    TreeFami TF324997.

    Miscellaneous databases

    ChiTaRSi LIPC. human.
    GeneWikii Hepatic_lipase.
    GenomeRNAii 3990.
    NextBioi 15652.
    PROi P11150.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11150.
    Bgeei P11150.
    CleanExi HS_LIPC.
    Genevestigatori P11150.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR002333. Lipase_hep.
    IPR008976. Lipase_LipOase.
    IPR013818. Lipase_N.
    IPR016272. Lipoprotein_lipase_LIPH.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    PTHR11610:SF2. PTHR11610:SF2. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00824. HEPLIPASE.
    PR00821. TAGLIPASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49723. SSF49723. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line."
      Stahnke G., Sprengel R., Augustin J., Will H.
      Differentiation 35:45-52(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-215 AND LEU-356.
      Tissue: Liver.
    2. "Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase."
      Datta S., Luo C.C., Li W.H., VanTuinen P., Ledbetter D.H., Brown M.A., Chen S.H., Liu S., Chan L.
      J. Biol. Chem. 263:1107-1110(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-215 AND LEU-356.
      Tissue: Liver.
    3. "Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase."
      Martin G.A., Busch S.J., Meredith G.D., Cardin A.D., Blankenship D.T., Mao S.J.T., Rechtin A.E., Woods C.W., Racke M.M., Schafer M.P., Fitzgerald M.C., Burke D.M., Flanagan M.A., Jackson R.L.
      J. Biol. Chem. 263:10907-10914(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT LEU-356.
      Tissue: Liver.
    4. "Structure of the human hepatic triglyceride lipase gene."
      Cai S.J., Wong D.M., Chen S.H., Chan L.
      Biochemistry 28:8966-8971(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-356.
    5. "Isolation and characterization of the human hepatic lipase gene."
      Ameis D., Stahnke G., Kobayashi J., McLean J., Lee G., Buscher M., Schotz M.C., Will H.
      J. Biol. Chem. 265:6552-6555(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-215 AND LEU-356.
    6. "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], VARIANTS SER-215 AND LEU-356.
      Tissue: Kidney and Thymus.
    7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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], VARIANT LEU-356.
    9. "18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3."
      Tiebel O., Gehrisch S., Pietzsch J., Gromeier S., Jaross W.
      Hum. Mutat. 12:216-216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-152, VARIANT HL DEFICIENCY HIS-TYR-THR-VAL-ALA-VAL-134 INS.
    10. "Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene."
      Takagi A., Ikeda Y., Mori A., Ashida Y., Yamamoto A.
      Mol. Cell. Probes 10:313-314(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 464-499.
    11. "The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish diabetes prevention study."
      Todorova B., Kubaszek A., Pihlajamaki J., Lindstrom J., Eriksson J., Valle T.T., Hamalainen H., Ilanne-Parikka P., Keinanen-Kiukaanniemi S., Tuomilehto J., Uusitupa M., Laakso M.
      J. Clin. Endocrinol. Metab. 89:2019-2023(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH NIDDM SUSCEPTIBILITY.
    12. "The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects."
      Grarup N., Andreasen C.H., Andersen M.K., Albrechtsen A., Sandbaek A., Lauritzen T., Borch-Johnsen K., Jorgensen T., Schmitz O., Hansen T., Pedersen O.
      J. Clin. Endocrinol. Metab. 93:2294-2299(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HDLCQ12.
    13. "Human hepatic lipase mutations and polymorphisms."
      Hegele R.A., Tu L., Connelly P.W.
      Hum. Mutat. 1:320-324(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HL DEFICIENCY PHE-289 AND MET-405.
    14. "Genetic variants affecting human lipoprotein and hepatic lipases."
      Hayden M.R., Ma Y., Brunzell J., Henderson H.E.
      Curr. Opin. Lipidol. 2:104-109(1991)
      Cited for: REVIEW ON POLYMORPHISM.
    15. Cited for: VARIANTS MET-95; SER-215 AND ASN-440.
    16. "Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
      Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
      Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MET-95; SER-215; PHE-289; ILE-342; LEU-356; MET-405 AND ALA-409.

    Entry informationi

    Entry nameiLIPC_HUMAN
    AccessioniPrimary (citable) accession number: P11150
    Secondary accession number(s): A2RUB4
    , A8K9B6, O43571, P78529, Q99465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 166 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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

    External Data

    Dasty 3