Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q05469

- LIPS_HUMAN

UniProt

Q05469 - LIPS_HUMAN

Protein

Hormone-sensitive lipase

Gene

LIPE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 4 (17 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.

    Catalytic activityi

    Diacylglycerol + H2O = monoacylglycerol + a carboxylate.
    Triacylglycerol + H2O = diacylglycerol + a carboxylate.
    Monoacylglycerol + H2O = glycerol + a carboxylate.

    Enzyme regulationi

    Rapidly activated by cAMP-dependent phosphorylation under the influence of catecholamines. Dephosphorylation and inactivation are controlled by insulin.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei651 – 6511PROSITE-ProRule annotation
    Active sitei725 – 7251PROSITE-ProRule annotation

    GO - Molecular functioni

    1. hormone-sensitive lipase activity Source: UniProtKB-EC
    2. protein binding Source: UniProtKB
    3. triglyceride lipase activity Source: Ensembl

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. diacylglycerol catabolic process Source: Ensembl
    3. lipid catabolic process Source: UniProtKB
    4. long-chain fatty acid catabolic process Source: Ensembl
    5. protein phosphorylation Source: ProtInc
    6. small molecule metabolic process Source: Reactome
    7. triglyceride catabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01328-MONOMER.
    BRENDAi3.1.1.79. 2681.
    ReactomeiREACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    UniPathwayiUPA00256.

    Protein family/group databases

    MEROPSiS09.993.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hormone-sensitive lipase (EC:3.1.1.79)
    Short name:
    HSL
    Gene namesi
    Name:LIPE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6621. LIPE.

    Subcellular locationi

    Cell membrane. Membranecaveola. Cytoplasmcytosol
    Note: Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin stimulation.

    GO - Cellular componenti

    1. caveola Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB-SubCell
    3. lipid particle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30393.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10761076Hormone-sensitive lipasePRO_0000071547Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei853 – 8531PhosphoserineBy similarity
    Modified residuei855 – 8551Phosphoserine; by AMPKBy similarity
    Modified residuei950 – 9501PhosphoserineBy similarity
    Modified residuei951 – 9511PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by AMPK may block translocation to lipid droplets.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05469.
    PaxDbiQ05469.
    PRIDEiQ05469.

    PTM databases

    PhosphoSiteiQ05469.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05469.
    BgeeiQ05469.
    CleanExiHS_LIPE.
    GenevestigatoriQ05469.

    Organism-specific databases

    HPAiCAB017700.

    Interactioni

    Subunit structurei

    Interacts with PTRF in the adipocyte cytoplasm. Interacts with PLIN5 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi110179. 3 interactions.
    IntActiQ05469. 1 interaction.
    MINTiMINT-1370154.
    STRINGi9606.ENSP00000244289.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05469.
    SMRiQ05469. Positions 636-826, 970-1059.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi651 – 6533Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

    Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Phylogenomic databases

    eggNOGiCOG0657.
    HOGENOMiHOG000047722.
    HOVERGENiHBG000187.
    InParanoidiQ05469.
    KOiK07188.
    OMAiLVVHIHG.
    OrthoDBiEOG7KSX7S.
    PhylomeDBiQ05469.
    TreeFamiTF314423.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR010468. HSL_N.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 2 hits.
    PF06350. HSL_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 2 hits.
    PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
    PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05469-1) [UniParc]FASTAAdd to Basket

    Also known as: Testicular

    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

    MEPGSKSVSR SDWQPEPHQR PITPLEPGPE KTPIAQPESK TLQGSNTQQK     50
    PASNQRPLTQ QETPAQHDAE SQKEPRAQQK SASQEEFLAP QKPAPQQSPY 100
    IQRVLLTQQE AASQQGPGLG KESITQQEPA LRQRHVAQPG PGPGEPPPAQ 150
    QEAESTPAAQ AKPGAKREPS APTESTSQET PEQSDKQTTP VQGAKSKQGS 200
    LTELGFLTKL QELSIQRSAL EWKALSEWVT DSESESDVGS SSDTDSPATM 250
    GGMVAQGVKL GFKGKSGYKV MSGYSGTSPH EKTSARNHRH YQDTASRLIH 300
    NMDLRTMTQS LVTLAEDNIA FFSSQGPGET AQRLSGVFAG VREQALGLEP 350
    ALGRLLGVAH LFDLDPETPA NGYRSLVHTA RCCLAHLLHK SRYVASNRRS 400
    IFFRTSHNLA ELEAYLAALT QLRALVYYAQ RLLVTNRPGV LFFEGDEGLT 450
    ADFLREYVTL HKGCFYGRCL GFQFTPAIRP FLQTISIGLV SFGEHYKRNE 500
    TGLSVAASSL FTSGRFAIDP ELRGAEFERI TQNLDVHFWK AFWNITEMEV 550
    LSSLANMASA TVRVSRLLSL PPEAFEMPLT ADPTLTVTIS PPLAHTGPGP 600
    VLVRLISYDL REGQDSEELS SLIKSNGQRS LELWPRPQQA PRSRSLIVHF 650
    HGGGFVAQTS RSHEPYLKSW AQELGAPIIS IDYSLAPEAP FPRALEECFF 700
    AYCWAIKHCA LLGSTGERIC LAGDSAGGNL CFTVALRAAA YGVRVPDGIM 750
    AAYPATMLQP AASPSRLLSL MDPLLPLSVL SKCVSAYAGA KTEDHSNSDQ 800
    KALGMMGLVR RDTALLLRDF RLGASSWLNS FLELSGRKSQ KMSEPIAEPM 850
    RRSVSEAALA QPQGPLGTDS LKNLTLRDLS LRGNSETSSD TPEMSLSAET 900
    LSPSTPSDVN FLLPPEDAGE EAEAKNELSP MDRGLGVRAA FPEGFHPRRS 950
    SQGATQMPLY SSPIVKNPFM SPLLAPDSML KSLPPVHIVA CALDPMLDDS 1000
    VMLARRLRNL GQPVTLRVVE DLPHGFLTLA ALCRETRQAA ELCVERIRLV 1050
    LTPPAGAGPS GETGAAGVDG GCGGRH 1076
    Length:1,076
    Mass (Da):116,598
    Last modified:April 17, 2007 - v4
    Checksum:i1CC0E3880FF64D74
    GO
    Isoform 2 (identifier: Q05469-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-301: Missing.

    Show »
    Length:775
    Mass (Da):84,128
    Checksum:i3462D4A99945661B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301T → A in AAA69810. (PubMed:8506334)Curated
    Sequence conflicti230 – 2301T → A in AAC50666. (PubMed:8812477)Curated
    Sequence conflicti230 – 2301T → A in ABA03168. 1 PublicationCurated
    Sequence conflicti486 – 4861S → Y in AAH70041. (PubMed:15489334)Curated
    Sequence conflicti608 – 6081Y → C in AAH70041. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001Y → H.1 Publication
    Corresponds to variant rs16975750 [ dbSNP | Ensembl ].
    VAR_025108
    Natural varianti127 – 1271Q → H.1 Publication
    Corresponds to variant rs34080774 [ dbSNP | Ensembl ].
    VAR_025109
    Natural varianti146 – 1461P → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036539
    Natural varianti146 – 1461P → S.1 Publication
    Corresponds to variant rs34348028 [ dbSNP | Ensembl ].
    VAR_025110
    Natural varianti177 – 1771S → T.1 Publication
    Corresponds to variant rs16975748 [ dbSNP | Ensembl ].
    VAR_025111
    Natural varianti194 – 1941A → V.1 Publication
    Corresponds to variant rs34996020 [ dbSNP | Ensembl ].
    VAR_025112
    Natural varianti217 – 2171R → Q.1 Publication
    Corresponds to variant rs3745238 [ dbSNP | Ensembl ].
    VAR_025113
    Natural varianti497 – 4971K → N.1 Publication
    Corresponds to variant rs35938529 [ dbSNP | Ensembl ].
    VAR_025114
    Natural varianti499 – 4991N → H.1 Publication
    Corresponds to variant rs33921216 [ dbSNP | Ensembl ].
    VAR_025115
    Natural varianti938 – 9381R → S.1 Publication
    Corresponds to variant rs7246232 [ dbSNP | Ensembl ].
    VAR_025116

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 301301Missing in isoform 2. CuratedVSP_017116Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11706 Genomic DNA. Translation: AAA69810.1.
    U40001 mRNA. Translation: AAC50666.1.
    DQ188033 Genomic DNA. Translation: ABA03168.1.
    BC070041 mRNA. Translation: AAH70041.1.
    CCDSiCCDS12607.1. [Q05469-1]
    RefSeqiNP_005348.2. NM_005357.3. [Q05469-1]
    XP_005258997.1. XM_005258940.2. [Q05469-2]
    XP_005258998.1. XM_005258941.2. [Q05469-2]
    XP_006723281.1. XM_006723218.1. [Q05469-2]
    UniGeneiHs.656980.

    Genome annotation databases

    EnsembliENST00000244289; ENSP00000244289; ENSG00000079435. [Q05469-1]
    GeneIDi3991.
    KEGGihsa:3991.
    UCSCiuc002otr.3. human. [Q05469-1]

    Polymorphism databases

    DMDMi145559491.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11706 Genomic DNA. Translation: AAA69810.1 .
    U40001 mRNA. Translation: AAC50666.1 .
    DQ188033 Genomic DNA. Translation: ABA03168.1 .
    BC070041 mRNA. Translation: AAH70041.1 .
    CCDSi CCDS12607.1. [Q05469-1 ]
    RefSeqi NP_005348.2. NM_005357.3. [Q05469-1 ]
    XP_005258997.1. XM_005258940.2. [Q05469-2 ]
    XP_005258998.1. XM_005258941.2. [Q05469-2 ]
    XP_006723281.1. XM_006723218.1. [Q05469-2 ]
    UniGenei Hs.656980.

    3D structure databases

    ProteinModelPortali Q05469.
    SMRi Q05469. Positions 636-826, 970-1059.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110179. 3 interactions.
    IntActi Q05469. 1 interaction.
    MINTi MINT-1370154.
    STRINGi 9606.ENSP00000244289.

    Chemistry

    BindingDBi Q05469.
    ChEMBLi CHEMBL3590.
    GuidetoPHARMACOLOGYi 2593.

    Protein family/group databases

    MEROPSi S09.993.

    PTM databases

    PhosphoSitei Q05469.

    Polymorphism databases

    DMDMi 145559491.

    Proteomic databases

    MaxQBi Q05469.
    PaxDbi Q05469.
    PRIDEi Q05469.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244289 ; ENSP00000244289 ; ENSG00000079435 . [Q05469-1 ]
    GeneIDi 3991.
    KEGGi hsa:3991.
    UCSCi uc002otr.3. human. [Q05469-1 ]

    Organism-specific databases

    CTDi 3991.
    GeneCardsi GC19M042906.
    H-InvDB HIX0040096.
    HGNCi HGNC:6621. LIPE.
    HPAi CAB017700.
    MIMi 151750. gene.
    neXtProti NX_Q05469.
    PharmGKBi PA30393.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0657.
    HOGENOMi HOG000047722.
    HOVERGENi HBG000187.
    InParanoidi Q05469.
    KOi K07188.
    OMAi LVVHIHG.
    OrthoDBi EOG7KSX7S.
    PhylomeDBi Q05469.
    TreeFami TF314423.

    Enzyme and pathway databases

    UniPathwayi UPA00256 .
    BioCyci MetaCyc:HS01328-MONOMER.
    BRENDAi 3.1.1.79. 2681.
    Reactomei REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

    Miscellaneous databases

    GeneWikii Hormone-sensitive_lipase.
    GenomeRNAii 3991.
    NextBioi 15656.
    PROi Q05469.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05469.
    Bgeei Q05469.
    CleanExi HS_LIPE.
    Genevestigatori Q05469.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR010468. HSL_N.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 2 hits.
    PF06350. HSL_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 2 hits.
    PROSITEi PS01173. LIPASE_GDXG_HIS. 1 hit.
    PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium."
      Langin D., Laurell H., Stenson Holst L., Belfrage P., Holm C.
      Proc. Natl. Acad. Sci. U.S.A. 90:4897-4901(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase."
      Holst L.S., Langin D., Mulder H., Laurell H., Grober J., Bergh A., Mohrenweiser H.W., Edgren G., Holm C.
      Genomics 35:441-447(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. SeattleSNPs variation discovery resource
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-100; HIS-127; SER-146; THR-177; VAL-194; GLN-217; ASN-497; HIS-499 AND SER-938.
    4. "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] (ISOFORM 1).
      Tissue: Testis.
    5. "Association and insulin regulated translocation of hormone-sensitive lipase with PTRF."
      Aboulaich N., Oertegren U., Vener A.V., Stralfors P.
      Biochem. Biophys. Res. Commun. 350:657-661(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTRF, SUBCELLULAR LOCATION.
    6. "Separation and characterization of caveolae subclasses in the plasma membrane of primary adipocytes; segregation of specific proteins and functions."
      Oertegren U., Yin L., Oest A., Karlsson H., Nystrom F.H., Stralfors P.
      FEBS J. 273:3381-3392(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "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.
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-146.

    Entry informationi

    Entry nameiLIPS_HUMAN
    AccessioniPrimary (citable) accession number: Q05469
    Secondary accession number(s): Q3LRT2, Q6NSL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 135 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3