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    LIPH lipase H [ Homo sapiens (human) ]

    Gene ID: 200879, updated on 17-Jun-2019

    Summary

    Official Symbol
    LIPHprovided by HGNC
    Official Full Name
    lipase Hprovided by HGNC
    Primary source
    HGNC:HGNC:18483
    See related
    Ensembl:ENSG00000163898 MIM:607365
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    AH; LAH2; ARWH2; HYPT7; LPDLR; PLA1B; mPA-PLA1
    Summary
    This gene encodes a membrane-bound member of the mammalian triglyceride lipase family. It catalyzes the production of 2-acyl lysophosphatidic acid (LPA), which is a lipid mediator with diverse biological properties that include platelet aggregation, smooth muscle contraction, and stimulation of cell proliferation and motility. [provided by RefSeq, Jul 2008]
    Expression
    Biased expression in colon (RPKM 18.6), stomach (RPKM 18.4) and 12 other tissues See more
    Orthologs

    Genomic context

    See LIPH in Genome Data Viewer
    Location:
    3q27.2
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    109.20190607 current GRCh38.p13 (GCF_000001405.39) 3 NC_000003.12 (185506262..185552661, complement)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (185225570..185270369, complement)

    Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene mitogen-activated protein kinase kinase kinase 13 Neighboring gene uncharacterized LOC105374254 Neighboring gene transmembrane protein 41A Neighboring gene uncharacterized LOC107986055 Neighboring gene SUMO specific peptidase 2 Neighboring gene ribosomal protein L34 pseudogene 10

    Genomic regions, transcripts, and products

    Expression

    • Project title: HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    Pathways from BioSystems

    • Digestion of dietary lipid, organism-specific biosystem (from REACTOME)
      Digestion of dietary lipid, organism-specific biosystemDietary lipids such as long-chain triacylglycerols and cholesterol esters are digested in the stomach and small intestine to yield long-chain fatty acids, monoacylglycerols, glycerol and cholesterol ...
    • Lipid digestion, mobilization, and transport, organism-specific biosystem (from REACTOME)
      Lipid digestion, mobilization, and transport, organism-specific biosystemProcesses annotated here include the digestion of dietary lipids, sterol uptake, the formation and turnover of lipoproteins (chylomicrons, VLDL, LDL, and HDL), and the mobilization of fatty acids thr...
    • Metabolism, organism-specific biosystem (from REACTOME)
      Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
    • Metabolism of lipids and lipoproteins, organism-specific biosystem (from REACTOME)
      Metabolism of lipids and lipoproteins, organism-specific biosystemLipids are hydrophobic but otherwise chemically diverse molecules that play a wide variety of roles in human biology. They include ketone bodies, fatty acids, triacylglycerols, phospholipids and sphi...

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    carboxylic ester hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
     
    heparin binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    lipase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    phospholipase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    phospholipase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    lipid catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    lipid catabolic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    phosphatidic acid biosynthetic process TAS
    Traceable Author Statement
    more info
     
    Component Evidence Code Pubs
    extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    extracellular space IDA
    Inferred from Direct Assay
    more info
    PubMed 
    plasma membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    plasma membrane TAS
    Traceable Author Statement
    more info
     

    General protein information

    Preferred Names
    lipase member H
    Names
    LPD lipase-related protein
    lipase, member H
    mPA-PLA1 alpha
    membrane-associated phosphatidic acid-selective phospholipase A1-alpha
    membrane-bound phosphatidic acid-selective phospholipase A1
    phospholipase A(1)
    phospholipase A1 member B
    NP_640341.1
    XP_006713592.1
    XP_011510832.1
    XP_011510833.1
    XP_016861341.1

    NCBI Reference Sequences (RefSeq)

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_012183.1 RefSeqGene

      Range
      5001..49800
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_139248.3NP_640341.1  lipase member H precursor

      See identical proteins and their annotated locations for NP_640341.1

      Status: REVIEWED

      Source sequence(s)
      AC099661, AK122651, BC064941, BI965988
      Consensus CDS
      CCDS3272.1
      UniProtKB/Swiss-Prot
      Q8WWY8
      Related
      ENSP00000296252.4, ENST00000296252.9
      Conserved Domains (1) summary
      cd00707
      Location:39303
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p13 Primary Assembly

    Genomic

    1. NC_000003.12 Reference GRCh38.p13 Primary Assembly

      Range
      185506262..185552661 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011512530.3XP_011510832.1  lipase member H isoform X3

      See identical proteins and their annotated locations for XP_011510832.1

      Conserved Domains (1) summary
      cd00707
      Location:1260
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
    2. XM_017005852.2XP_016861341.1  lipase member H isoform X2

      UniProtKB/TrEMBL
      A2IBA6
      Related
      ENSP00000396384.2, ENST00000424591.6
      Conserved Domains (1) summary
      cd00707
      Location:39269
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
    3. XM_006713529.4XP_006713592.1  lipase member H isoform X1

      Conserved Domains (1) summary
      cd00707
      Location:39273
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
    4. XM_011512531.3XP_011510833.1  lipase member H isoform X3

      See identical proteins and their annotated locations for XP_011510833.1

      Conserved Domains (1) summary
      cd00707
      Location:1260
      Pancreat_lipase_like; Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the ...
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