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Q05469

- LIPS_HUMAN

UniProt

Q05469 - LIPS_HUMAN

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Protein

Hormone-sensitive lipase

Gene
LIPE
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 6511 Reviewed prediction
Active sitei725 – 7251 Reviewed prediction

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
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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 – 8531Phosphoserine By similarity
Modified residuei855 – 8551Phosphoserine; by AMPK By similarity
Modified residuei950 – 9501Phosphoserine By similarity
Modified residuei951 – 9511Phosphoserine By 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.1 Publication

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.

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 hole By similarity

Sequence similaritiesi

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

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. VSP_017116Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301T → A in AAA69810. 1 Publication
Sequence conflicti230 – 2301T → A in AAC50666. 1 Publication
Sequence conflicti230 – 2301T → A in ABA03168. 1 Publication
Sequence conflicti486 – 4861S → Y in AAH70041. 1 Publication
Sequence conflicti608 – 6081Y → C in AAH70041. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 134 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

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