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P06858

- LIPL_HUMAN

UniProt

P06858 - LIPL_HUMAN

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Protein

Lipoprotein lipase

Gene

LPL

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Nucleophile
Active sitei183 – 1831Charge relay system
Active sitei268 – 2681Charge relay system

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. heparin binding Source: BHF-UCL
  3. lipoprotein lipase activity Source: BHF-UCL
  4. phospholipase activity Source: BHF-UCL
  5. receptor binding Source: BHF-UCL
  6. triglyceride binding Source: Ensembl
  7. triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

  1. chylomicron remodeling Source: BHF-UCL
  2. fatty acid biosynthetic process Source: BHF-UCL
  3. lipoprotein metabolic process Source: Reactome
  4. phospholipid metabolic process Source: BHF-UCL
  5. phototransduction, visible light Source: Reactome
  6. positive regulation of cholesterol storage Source: BHF-UCL
  7. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  8. positive regulation of sequestering of triglyceride Source: BHF-UCL
  9. response to cold Source: Ensembl
  10. response to drug Source: Ensembl
  11. retinoid metabolic process Source: Reactome
  12. small molecule metabolic process Source: Reactome
  13. triglyceride biosynthetic process Source: Ensembl
  14. triglyceride catabolic process Source: BHF-UCL
  15. triglyceride homeostasis Source: BHF-UCL
  16. triglyceride metabolic process Source: BHF-UCL
  17. very-low-density lipoprotein particle remodeling Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BRENDAi3.1.1.34. 2681.
ReactomeiREACT_24968. Retinoid metabolism and transport.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_6841. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoprotein lipase (EC:3.1.1.34)
Short name:
LPL
Gene namesi
Name:LPL
Synonyms:LIPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:6677. LPL.

Subcellular locationi

Cell membrane By similarity; Lipid-anchor › GPI-anchor By similarity. Secreted By similarity
Note: Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity).By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. chylomicron Source: UniProtKB-KW
  4. extracellular matrix Source: Ensembl
  5. extracellular region Source: Reactome
  6. extracellular space Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProtKB
  8. plasma membrane Source: UniProtKB-SubCell
  9. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, Membrane, Secreted, VLDL

Pathology & Biotechi

Involvement in diseasei

Lipoprotein lipase deficiency (LPL deficiency)
[MIM:238600]: Recessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.54 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 Publications
Corresponds to variant rs1801177 [ dbSNP | Ensembl ].		VAR_011948
Natural varianti70 – 701N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications
VAR_057914
Natural varianti96 – 961V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication
VAR_057915
Natural varianti98 – 981A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057916
Natural varianti102 – 1021R → S in LPL deficiency. 1 Publication
VAR_004211
Natural varianti113 – 1131W → G in LPL deficiency.
VAR_004212
Natural varianti113 – 1131W → R in LPL deficiency. 2 Publications
VAR_004213
Natural varianti128 – 1281T → A in LPL deficiency. 2 Publications
VAR_057917
Natural varianti132 – 1321G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057918
Natural varianti163 – 1631H → R in LPL deficiency. 1 Publication
VAR_004214
Natural varianti169 – 1691G → E in LPL deficiency; loss of activity. 1 Publication
VAR_004215
Natural varianti181 – 1811G → S in LPL deficiency. 1 Publication
VAR_004216
Natural varianti181 – 1811G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057919
Natural varianti183 – 1831D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications
VAR_004217
Natural varianti183 – 1831D → H in LPL deficiency. 1 Publication
VAR_057920
Natural varianti183 – 1831D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 1 Publication
VAR_004218
Natural varianti184 – 1841P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication
VAR_004219
Natural varianti185 – 1851A → T in LPL deficiency; 3.2% of activity.
VAR_004220
Natural varianti186 – 1861G → E in LPL deficiency. 1 Publication
VAR_057921
Natural varianti190 – 1901E → G in LPL deficiency. 1 Publication
VAR_057922
Natural varianti199 – 1991S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 Publications
VAR_004221
Natural varianti201 – 2011D → V in LPL deficiency. 1 Publication
VAR_057923
Natural varianti203 – 2031A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication
VAR_004222
Natural varianti207 – 2071D → E in LPL deficiency. 1 Publication
VAR_004223
Natural varianti208 – 2081V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057924
Natural varianti210 – 2101H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication
VAR_057925
Natural varianti210 – 2101H → Q in LPL deficiency; loss of activity.
VAR_004224
Natural varianti215 – 2151G → E in LPL deficiency; loss of activity. 12 Publications
VAR_004225
Natural varianti215 – 2151G → R in LPL deficiency. 2 Publications
VAR_057926
Natural varianti220 – 2201S → R in LPL deficiency; 2.0% of activity.
VAR_004226
Natural varianti221 – 2211I → T in LPL deficiency; loss of activity. 5 Publications
VAR_004227
Natural varianti222 – 2221G → E in LPL deficiency. 1 Publication
VAR_004228
Natural varianti225 – 2251K → R in LPL deficiency. 1 Publication
VAR_057927
Natural varianti227 – 2271V → A in LPL deficiency. 1 Publication
VAR_057928
Natural varianti231 – 2311D → E in LPL deficiency; loss of activity. 3 Publications
VAR_004229
Natural varianti232 – 2321I → S in LPL deficiency. 1 Publication
VAR_004230
Natural varianti234 – 2341P → L in LPL deficiency; loss of activity. 2 Publications
VAR_004231
Natural varianti243 – 2431C → S in LPL deficiency; loss of activity. 1 Publication
VAR_004232
Natural varianti252 – 2521I → T in LPL deficiency. 1 Publication
VAR_057929
Natural varianti266 – 2661C → W in LPL deficiency. 1 Publication
VAR_057930
Natural varianti270 – 2701R → C in LPL deficiency. 4 Publications
VAR_057931
Natural varianti270 – 2701R → H in LPL deficiency; loss of activity. 6 Publications
VAR_004233
Natural varianti271 – 2711S → T in LPL deficiency. 1 Publication
Corresponds to variant rs28934893 [ dbSNP | Ensembl ].		VAR_004234
Natural varianti277 – 2771D → N in LPL deficiency; 5% of full activity. 5 Publications
VAR_004235
Natural varianti278 – 2781S → C in LPL deficiency.
VAR_004236
Natural varianti279 – 2791L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 Publications
Corresponds to variant rs35414700 [ dbSNP | Ensembl ].		VAR_057932
Natural varianti279 – 2791L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057933
Natural varianti286 – 2861S → G in LPL deficiency. 1 Publication
VAR_004237
Natural varianti286 – 2861S → R in LPL deficiency. 1 Publication
VAR_004238
Natural varianti288 – 2881A → T Associated with LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 Publications
Corresponds to variant rs1800011 [ dbSNP | Ensembl ].		VAR_011949
Natural varianti289 – 2891Y → H in LPL deficiency; no enzyme activity. 1 Publication
VAR_057934
Natural varianti297 – 2971F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications
VAR_057935
Natural varianti303 – 3031L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication
VAR_057936
Natural varianti305 – 3051C → R in LPL deficiency. 1 Publication
VAR_057937
Natural varianti310 – 3101C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057938
Natural varianti313 – 3131L → P in LPL deficiency. 1 Publication
VAR_057939
Natural varianti318 – 3181N → S in LPL deficiency; loss of activity; frequent mutation. 8 Publications
Corresponds to variant rs268 [ dbSNP | Ensembl ].		VAR_004239
Natural varianti325 – 3251S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057940
Natural varianti328 – 3281M → R in LPL deficiency. 1 Publication
VAR_057941
Natural varianti328 – 3281M → T in LPL deficiency.
VAR_004240
Natural varianti330 – 3301L → F in LPL deficiency. 1 Publication
VAR_057942
Natural varianti330 – 3301L → P in LPL deficiency.
VAR_004241
Natural varianti361 – 3611A → T in LPL deficiency. 2 Publications
VAR_004242
Natural varianti365 – 3651S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057943
Natural varianti392 – 3921L → V in LPL deficiency; loss of activity. 1 Publication
VAR_004243
Natural varianti423 – 4242Missing in LPL deficiency; affects the protein folding.
VAR_004244
Natural varianti437 – 4371E → K in LPL deficiency. 1 Publication
VAR_004245
Natural varianti437 – 4371E → V in LPL deficiency. 1 Publication
VAR_004246
Natural varianti445 – 4451C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 Publication
VAR_057944
Natural varianti448 – 4481E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication
VAR_057945

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591S → G: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi159 – 1591S → T: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi268 – 2681H → G: Lacks both triolein and tributyrin esterase activities. 1 Publication
Mutagenesisi268 – 2681H → Q: Lacks both triolein and tributyrin esterase activities. 1 Publication

Keywords - Diseasei

Disease mutation, Hyperlipidemia

Organism-specific databases

MIMi238600. phenotype.
Orphaneti309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBiPA232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 475448Lipoprotein lipasePRO_0000017775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Modified residuei121 – 1211Nitrated tyrosineBy similarity
Modified residuei191 – 1911Nitrated tyrosineBy similarity
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343 – 3431Nitrated tyrosineBy similarity
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

MaxQBiP06858.
PaxDbiP06858.
PRIDEiP06858.

PTM databases

PhosphoSiteiP06858.

Expressioni

Gene expression databases

BgeeiP06858.
CleanExiHS_LPL.
ExpressionAtlasiP06858. baseline and differential.
GenevestigatoriP06858.

Organism-specific databases

HPAiHPA048749.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1.By similarity1 Publication

Protein-protein interaction databases

BioGridi110205. 19 interactions.
IntActiP06858. 11 interactions.
MINTiMINT-1369348.
STRINGi9606.ENSP00000309757.

Structurei

3D structure databases

ProteinModelPortaliP06858.
SMRiP06858. Positions 36-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 464124PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni346 – 44196Heparin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP06858.
KOiK01059.
OMAiESVANCH.
PhylomeDBiP06858.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR03230. lipo_lipase. 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.

P06858-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA 
        60         70         80         90        100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY 
       110        120        130        140        150
KREPDSNVIV VDWLSRAQEH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL 
       160        170        180        190        200
DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP 
       210        220        230        240        250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR 
       260        270        280        290        300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG 
       310        320        330        340        350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS 
       360        370        380        390        400
GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG 
       410        420        430        440        450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV 
       460        470 
SHLQKGKAPA VFVKCHDKSL NKKSG
Length:475
Mass (Da):53,162
Last modified:January 1, 1988 - v1
Checksum:iFBD00FCD334FB8AA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 Publications
Corresponds to variant rs1801177 [ dbSNP | Ensembl ].		VAR_011948
Natural varianti70 – 701N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications
VAR_057914
Natural varianti71 – 711H → Q.
Corresponds to variant rs11542065 [ dbSNP | Ensembl ].		VAR_049819
Natural varianti96 – 961V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication
VAR_057915
Natural varianti98 – 981A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057916
Natural varianti102 – 1021R → S in LPL deficiency. 1 Publication
VAR_004211
Natural varianti113 – 1131W → G in LPL deficiency.
VAR_004212
Natural varianti113 – 1131W → R in LPL deficiency. 2 Publications
VAR_004213
Natural varianti128 – 1281T → A in LPL deficiency. 2 Publications
VAR_057917
Natural varianti132 – 1321G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057918
Natural varianti163 – 1631H → R in LPL deficiency. 1 Publication
VAR_004214
Natural varianti169 – 1691G → E in LPL deficiency; loss of activity. 1 Publication
VAR_004215
Natural varianti181 – 1811G → S in LPL deficiency. 1 Publication
VAR_004216
Natural varianti181 – 1811G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications
VAR_057919
Natural varianti183 – 1831D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 Publications
VAR_004217
Natural varianti183 – 1831D → H in LPL deficiency. 1 Publication
VAR_057920
Natural varianti183 – 1831D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 1 Publication
VAR_004218
Natural varianti184 – 1841P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication
VAR_004219
Natural varianti185 – 1851A → T in LPL deficiency; 3.2% of activity.
VAR_004220
Natural varianti186 – 1861G → E in LPL deficiency. 1 Publication
VAR_057921
Natural varianti190 – 1901E → G in LPL deficiency. 1 Publication
VAR_057922
Natural varianti199 – 1991S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 Publications
VAR_004221
Natural varianti201 – 2011D → V in LPL deficiency. 1 Publication
VAR_057923
Natural varianti203 – 2031A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication
VAR_004222
Natural varianti207 – 2071D → E in LPL deficiency. 1 Publication
VAR_004223
Natural varianti208 – 2081V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057924
Natural varianti210 – 2101H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication
VAR_057925
Natural varianti210 – 2101H → Q in LPL deficiency; loss of activity.
VAR_004224
Natural varianti215 – 2151G → E in LPL deficiency; loss of activity. 12 Publications
VAR_004225
Natural varianti215 – 2151G → R in LPL deficiency. 2 Publications
VAR_057926
Natural varianti220 – 2201S → R in LPL deficiency; 2.0% of activity.
VAR_004226
Natural varianti221 – 2211I → T in LPL deficiency; loss of activity. 5 Publications
VAR_004227
Natural varianti222 – 2221G → E in LPL deficiency. 1 Publication
VAR_004228
Natural varianti225 – 2251K → R in LPL deficiency. 1 Publication
VAR_057927
Natural varianti227 – 2271V → A in LPL deficiency. 1 Publication
VAR_057928
Natural varianti231 – 2311D → E in LPL deficiency; loss of activity. 3 Publications
VAR_004229
Natural varianti232 – 2321I → S in LPL deficiency. 1 Publication
VAR_004230
Natural varianti234 – 2341P → L in LPL deficiency; loss of activity. 2 Publications
VAR_004231
Natural varianti243 – 2431C → S in LPL deficiency; loss of activity. 1 Publication
VAR_004232
Natural varianti252 – 2521I → T in LPL deficiency. 1 Publication
VAR_057929
Natural varianti266 – 2661C → W in LPL deficiency. 1 Publication
VAR_057930
Natural varianti270 – 2701R → C in LPL deficiency. 4 Publications
VAR_057931
Natural varianti270 – 2701R → H in LPL deficiency; loss of activity. 6 Publications
VAR_004233
Natural varianti271 – 2711S → T in LPL deficiency. 1 Publication
Corresponds to variant rs28934893 [ dbSNP | Ensembl ].		VAR_004234
Natural varianti277 – 2771D → N in LPL deficiency; 5% of full activity. 5 Publications
VAR_004235
Natural varianti278 – 2781S → C in LPL deficiency.
VAR_004236
Natural varianti279 – 2791L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 Publications
Corresponds to variant rs35414700 [ dbSNP | Ensembl ].		VAR_057932
Natural varianti279 – 2791L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057933
Natural varianti286 – 2861S → G in LPL deficiency. 1 Publication
VAR_004237
Natural varianti286 – 2861S → R in LPL deficiency. 1 Publication
VAR_004238
Natural varianti288 – 2881A → T Associated with LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 Publications
Corresponds to variant rs1800011 [ dbSNP | Ensembl ].		VAR_011949
Natural varianti289 – 2891Y → H in LPL deficiency; no enzyme activity. 1 Publication
VAR_057934
Natural varianti297 – 2971F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications
VAR_057935
Natural varianti303 – 3031L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication
VAR_057936
Natural varianti305 – 3051C → R in LPL deficiency. 1 Publication
VAR_057937
Natural varianti310 – 3101C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057938
Natural varianti313 – 3131L → P in LPL deficiency. 1 Publication
VAR_057939
Natural varianti318 – 3181N → S in LPL deficiency; loss of activity; frequent mutation. 8 Publications
Corresponds to variant rs268 [ dbSNP | Ensembl ].		VAR_004239
Natural varianti325 – 3251S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057940
Natural varianti328 – 3281M → R in LPL deficiency. 1 Publication
VAR_057941
Natural varianti328 – 3281M → T in LPL deficiency.
VAR_004240
Natural varianti330 – 3301L → F in LPL deficiency. 1 Publication
VAR_057942
Natural varianti330 – 3301L → P in LPL deficiency.
VAR_004241
Natural varianti361 – 3611A → T in LPL deficiency. 2 Publications
VAR_004242
Natural varianti365 – 3651S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication
VAR_057943
Natural varianti370 – 3701V → M.1 Publication
Corresponds to variant rs298 [ dbSNP | Ensembl ].		VAR_011950
Natural varianti379 – 3791T → A.1 Publication
Corresponds to variant rs300 [ dbSNP | Ensembl ].		VAR_011951
Natural varianti392 – 3921L → V in LPL deficiency; loss of activity. 1 Publication
VAR_004243
Natural varianti423 – 4242Missing in LPL deficiency; affects the protein folding.
VAR_004244
Natural varianti427 – 4271A → T.1 Publication
Corresponds to variant rs5934 [ dbSNP | Ensembl ].		VAR_011952
Natural varianti437 – 4371E → K in LPL deficiency. 1 Publication
VAR_004245
Natural varianti437 – 4371E → V in LPL deficiency. 1 Publication
VAR_004246
Natural varianti445 – 4451C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. 1 Publication
VAR_057944
Natural varianti448 – 4481E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication
VAR_057945

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15856 mRNA. Translation: AAB59536.1.
X14390 mRNA. Translation: CAA32564.1.
X54516 mRNA. Translation: CAA38372.1.
M76722 Genomic DNA. Translation: AAA59528.1.
S76076 Genomic DNA. Translation: AAB21000.1.
S76077 Genomic DNA. Translation: AAB20999.1.
BT006726 mRNA. Translation: AAP35372.1.
AK312311 mRNA. Translation: BAG35236.1.
CH471080 Genomic DNA. Translation: EAW63764.1.
BC011353 mRNA. Translation: AAH11353.1.
X68111 Genomic DNA. Translation: CAA48230.1.
CCDSiCCDS6012.1.
PIRiA26082. LIHUL.
RefSeqiNP_000228.1. NM_000237.2.
UniGeneiHs.180878.

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445.
GeneIDi4023.
KEGGihsa:4023.
UCSCiuc003wzk.4. human.

Polymorphism databases

DMDMi126314.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database
Wikipedia

Lipoprotein lipase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 M15856 mRNA. Translation: AAB59536.1 .
X14390 mRNA. Translation: CAA32564.1 .
X54516 mRNA. Translation: CAA38372.1 .
M76722 Genomic DNA. Translation: AAA59528.1 .
S76076 Genomic DNA. Translation: AAB21000.1 .
S76077 Genomic DNA. Translation: AAB20999.1 .
BT006726 mRNA. Translation: AAP35372.1 .
AK312311 mRNA. Translation: BAG35236.1 .
CH471080 Genomic DNA. Translation: EAW63764.1 .
BC011353 mRNA. Translation: AAH11353.1 .
X68111 Genomic DNA. Translation: CAA48230.1 .
CCDSi CCDS6012.1.
PIRi A26082. LIHUL.
RefSeqi NP_000228.1. NM_000237.2.
UniGenei Hs.180878.

3D structure databases

ProteinModelPortali P06858.
SMRi P06858. Positions 36-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110205. 19 interactions.
IntActi P06858. 11 interactions.
MINTi MINT-1369348.
STRINGi 9606.ENSP00000309757.

Chemistry

BindingDBi P06858.
ChEMBLi CHEMBL2060.
DrugBanki DB05269. AST-120.
DB06439. Tyloxapol.

PTM databases

PhosphoSitei P06858.

Polymorphism databases

DMDMi 126314.

Proteomic databases

MaxQBi P06858.
PaxDbi P06858.
PRIDEi P06858.

Protocols and materials databases

DNASUi 4023.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311322 ; ENSP00000309757 ; ENSG00000175445 .
GeneIDi 4023.
KEGGi hsa:4023.
UCSCi uc003wzk.4. human.

Organism-specific databases

CTDi 4023.
GeneCardsi GC08P019759.
GeneReviewsi LPL.
HGNCi HGNC:6677. LPL.
HPAi HPA048749.
MIMi 238600. phenotype.
609708. gene.
neXtProti NX_P06858.
Orphaneti 309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBi PA232.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00760000119069.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi P06858.
KOi K01059.
OMAi ESVANCH.
PhylomeDBi P06858.
TreeFami TF324997.

Enzyme and pathway databases

BRENDAi 3.1.1.34. 2681.
Reactomei REACT_24968. Retinoid metabolism and transport.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_6841. Chylomicron-mediated lipid transport.

Miscellaneous databases

GeneWikii Lipoprotein_lipase.
GenomeRNAii 4023.
NextBioi 15776.
PROi P06858.
SOURCEi Search...

Gene expression databases

Bgeei P06858.
CleanExi HS_LPL.
ExpressionAtlasi P06858. baseline and differential.
Genevestigatori P06858.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsi TIGR03230. lipo_lipase. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library."
    Gotoda T., Senda M., Gamou T., Furuichi Y., Oka K.
    Nucleic Acids Res. 17:2351-2352(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. "DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells."
    Takagi A., Ikeda Y., Yamamoto A.
    Nucleic Acids Res. 18:6436-6436(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence."
    Chuat J.-C., Raisonnier A., Etienne J., Galibert F.
    Gene 110:257-261(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-318.
  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].
    Tissue: Cerebellum.
  7. 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 SER-318.
    Tissue: Brain.
  9. "Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis."
    Enerbaeck S., Ohlsson B.G., Samuelsson L., Bjursell G.
    Mol. Cell. Biol. 12:4622-4633(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
  10. "Rapid and simple isolation procedure for lipoprotein lipase from human milk."
    Zechner R.
    Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-44.
    Tissue: Milk.
  11. "Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
    Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
    J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY.
  12. "Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution."
    Gin P., Beigneux A.P., Davies B., Young M.F., Ryan R.O., Bensadoun A., Fong L.G., Young S.G.
    Biochim. Biophys. Acta 1771:1464-1468(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPIHBP1.
  13. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
    Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
    Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70.
    Tissue: Milk.
  14. "Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray structure: consequences for heparin binding and catalysis."
    van Tilbeurgh H., Roussel A., Lalouel J.-M., Cambillau C.
    J. Biol. Chem. 269:4626-4633(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  15. "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 VARIANTS.
  16. "Compound heterozygote for lipoprotein lipase deficiency: Ser-->Thr244 and transition in 3' splice site of intron 2 (AG-->AA) in the lipoprotein lipase gene."
    Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H., Lalouel J.-M.
    Am. J. Hum. Genet. 47:721-726(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY THR-271.
  17. "Missense mutation (Gly-->Glu188) of human lipoprotein lipase imparting functional deficiency."
    Emi M., Wilson D.E., Iverius P.H., Wiu L., Hata A., Hegele R., Williams R.R., Lalouel J.-M.
    J. Biol. Chem. 265:5910-5916(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLU-215.
  18. "A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries."
    Monsalve M.V., Henderson H., Roederer G., Julien P., Deeb S., Kastelein J.J.P., Peritz L., Devlin R., Bruin T., Murthy M.R.V., Gagne C., Davignon J., Lupien P.J., Brunzell J.D., Hayden M.R.
    J. Clin. Invest. 86:728-734(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLU-215.
  19. "Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
    Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
    Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY THR-203.
  20. "Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome."
    Dichek H.L., Fojo S.S., Beg O.U., Skarlatos S.I., Brunzell J.D., Cutler G.B. Jr., Brewer H.B. Jr.
    J. Biol. Chem. 266:473-477(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY THR-221 AND HIS-270.
  21. "Catalytic triad residue mutation (Asp156-->Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447-->Ter) in a Turkish family."
    Faustinella F., Chang A., van Biervliet J.P., Rosseneu M., Vinaimont N., Smith L.C., Chen S.-H., Chan L.
    J. Biol. Chem. 266:14418-14424(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLY-183.
  22. "Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene."
    Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J., Kane J.P., Lee G., Wong H., Havel R.J., Schotz M.C.
    J. Clin. Invest. 87:1165-1170(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLU-169.
  23. "Amino acid substitution (Ile194-->Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin."
    Henderson H.E., Ma Y., Hassan F., Monsalve M.V., Marais A.D., Winkler F., Gubernator K., Peterson J., Brunzell J.D., Hayden M.R.
    J. Clin. Invest. 87:2005-2011(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY THR-221.
  24. "Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency."
    Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S., Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.
    J. Clin. Invest. 88:1856-1864(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLU-231 AND HIS-270, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY GLU-231 AND HIS-270.
  25. "A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians."
    Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V., Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J., Lupien P.J., Brunzell J., Hayden M.R.
    N. Engl. J. Med. 324:1761-1766(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY LEU-234.
  26. "A missense mutation (Trp86-->Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia."
    Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K., Chan L.
    Am. J. Hum. Genet. 50:1275-1280(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY ARG-113.
  27. "A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity."
    Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E., Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.
    Eur. J. Biochem. 208:267-272(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY ARG-184.
  28. "A missense mutation (Asp250-->Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries."
    Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G., Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J., Brunzell J.D., Hayden M.R.
    Genomics 13:649-653(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY ASN-277.
  29. "Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis."
    Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S., Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.
    J. Biol. Chem. 267:1918-1923(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ASN-183; GLY-183 AND SER-243.
  30. "Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
    Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
    J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268.
  31. "Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization."
    Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K., Shuhua J., Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H., Wilson D.E., Lalouel J.-M.
    J. Biol. Chem. 267:20132-20139(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLU-222.
  32. "A missense (Asp250-->Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency."
    Ishimura-Oka K., Semenkovich C.F., Faustinella F., Goldberg I.J., Shachter N., Smith L.C., Coleman T., Hide W.A., Brown W.V., Oka K.
    J. Lipid Res. 33:745-754(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLU-215; HIS-270 AND ASN-277.
  33. "Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes."
    Reina M., Brunzell J.D., Deeb S.S.
    J. Lipid Res. 33:1823-1832(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ARG-113; ARG-163; GLU-215; THR-221 AND SER-232.
  34. "A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia."
    Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.
    Biochem. Biophys. Res. Commun. 191:1046-1054(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY THR-361.
  35. "A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia)."
    Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K., Hofler G., Kostner G.M., Breslow J.L., Zechner R.
    Genomics 18:392-396(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY GLU-207.
  36. "Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene."
    Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D., Hayden M.R.
    J. Clin. Invest. 91:1953-1958(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY CYS-199.
  37. "Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes."
    Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N., Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.
    J. Clin. Invest. 92:203-211(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-102.
  38. "Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase."
    Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N., Brunzell J.D., Hayden M.R., Kastelein J.J.
    J. Lipid Res. 34:2109-2119(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-181.
  39. "A new Italian case of lipoprotein lipase deficiency: a Leu365-> Val change resulting in loss of enzyme activity."
    Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M., Collacicco A.M., Capurso A.
    Biochem. Biophys. Res. Commun. 199:570-576(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY VAL-392.
  40. "A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion."
    Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N., Yoshida S., Saito Y., Fojo S.S., Brewer H.B. Jr.
    Biochem. Biophys. Res. Commun. 205:506-515(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-70, CHARACTERIZATION OF VARIANT LPL DEFICIENCY SER-70.
  41. "Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries."
    Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P., Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S., Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D., Hayden M.R.
    Hum. Mutat. 3:52-58(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY HIS-270 AND CYS-270.
  42. "A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression."
    Bruin T., Tuzgoel S., Mulder W.J., van den Ende A.E., Jansen H., Hayden M.R., Kastelein J.J.P.
    J. Lipid Res. 35:438-445(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY LEU-96 AND GLU-215, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LEU-96.
  43. "High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform."
    Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L., Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.
    J. Lipid Res. 35:1066-1075(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY CYS-199; ARG-279; THR-288 AND SER-318, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ARG-279 AND THR-288.
  44. "A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia."
    Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D., Santamarina-Fojo S., Brewer H.B. Jr.
    J. Lipid Res. 35:1552-1560(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY VAL-437.
  45. "A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis."
    Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I., Jansen H., Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J., Hayden M.R.
    Nat. Genet. 10:28-34(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-318.
  46. "A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase."
    Henderson H.E., Hassan F., Marais D., Hayden M.R.
    Biochem. Biophys. Res. Commun. 227:189-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY TYR-445, CHARACTERIZATION OF VARIANT LPL DEFICIENCY TYR-445.
  47. "Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia."
    de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R., Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.
    Eur. J. Clin. Invest. 26:631-639(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-318, VARIANT ASN-36.
  48. "Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia."
    Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A., Kastelein J.J.P., Assmann G.
    Hum. Mutat. 8:381-383(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ASN-277 AND LYS-437.
  49. "A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia."
    Wiebusch H., Funke H., Santer R., Richter W., Assmann G.
    Hum. Mutat. 8:392-392(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLY-190 AND GLU-215.
  50. "Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."
    Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
    J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY HIS-289, VARIANT ASN-36, CHARACTERIZATION OF VARIANT LPL DEFICIENCY HIS-289, CHARACTERIZATION OF VARIANT ASN-36.
  51. "Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene."
    Benlian P., De Gennes J.L., Foubert L., Zhang H., Gagne S.E., Hayden M.
    N. Engl. J. Med. 335:848-854(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313.
  52. "A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry."
    Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J., Kastelein J.J., Benlian P., Hayden M.R.
    Hum. Mutat. 10:179-185(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY ARG-286.
  53. "Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy."
    Mailly F., Palmen J., Muller D.P.R., Gibbs T., Lloyd J., Brunzell J., Durrington P., Mitropoulos K., Betteridge J., Watts G., Lithell H., Angelico F., Humphries S.E., Talmud P.J.
    Hum. Mutat. 10:465-473(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS.
  54. "Assessment of French patients with LPL deficiency for French Canadian mutations."
    Foubert L., De Gennes J.L., Lagarde J.P., Ehrenborg E., Raisonnier A., Girardet J.P., Hayden M.R., Benlian P.
    J. Med. Genet. 34:672-675(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND ASN-277.
  55. "Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event."
    Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T., Erkelens D.W., Hayden M.R., Kastelein J.J.P.
    Am. J. Med. Genet. 78:313-316(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY THR-252 AND HIS-270.
  56. "A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis."
    Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.
    Clin. Chim. Acta 269:1-12(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY LYS-448, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LYS-448.
  57. "Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LPL) as a cause of chylomicronemia."
    Evans D., Wendt D., Ahle S., Guerra A., Beisiegel U.
    Hum. Mutat. 12:217-217(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLU-215 AND GLY-286.
  58. "Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
    Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
    Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY SER-318, VARIANTS ASN-36 AND THR-288.
  59. Cited for: VARIANT LPL DEFICIENCY SER-318, VARIANTS MET-370 AND ALA-379.
  60. Cited for: VARIANT THR-427.
  61. Erratum
    Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
    Nat. Genet. 23:373-373(1999)
  62. "A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency."
    Takagi A., Ikeda Y., Takeda E., Yamamoto A.
    Biochim. Biophys. Acta 1502:433-446(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY LEU-297, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LEU-297.
  63. "A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia."
    Ikeda Y., Goji K., Takagi A.
    Clin. Sci. 99:569-578(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY ARG-132 AND GLU-231, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ARG-132 AND GLU-231.
  64. "Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis."
    Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K., Maerz W., Haering H.-U., Matthaei S.
    J. Clin. Endocrinol. Metab. 85:4795-4798(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY TRP-266.
  65. "Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23."
    Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J., Sandhofer F., Paulweber B.
    J. Lipid Res. 41:734-741(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY ASP-210, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ASP-210.
  66. "Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8."
    Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K., Nishi Y., Yamamoto A.
    J. Lipid Res. 42:1072-1081(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY VAL-181, CHARACTERIZATION OF VARIANT LPL DEFICIENCY VAL-181.
  67. "Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia."
    Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L., Masarei J.R.L., Pang C.-P.
    Hum. Mutat. 20:232-233(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365.
  68. "Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis."
    Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
    Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY PHE-303, CHARACTERIZATION OF VARIANT LPL DEFICIENCY PHE-303.
  69. "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: VARIANT LPL DEFICIENCY SER-318, VARIANT ASN-36.
  70. "Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method."
    Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A., Chouery E., Salem N., Junien C., Aydenian H., Boileau C.
    Clin. Genet. 65:158-161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPL DEFICIENCY VAL-201.
  71. "Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical and genetic study."
    Kavazarakis E., Stabouli S., Gourgiotis D., Roumeliotou K., Traeger-Synodinos J., Bossios A., Fretzayas A., Kanavakis E.
    Eur. J. Pediatr. 163:462-466(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLU-215 AND ARG-328.
  72. "Mutations in Japanese subjects with primary hyperlipidemia -- results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996."
    The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan
    Maruyama T., Yamashita S., Matsuzawa Y., Bujo H., Takahashi K., Saito Y., Ishibashi S., Ohashi K., Shionoiri F., Gotoda T., Yamada N., Kita T.
    J. Atheroscler. Thromb. 11:131-145(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY SER-70; ARG-132; VAL-181; GLU-215; THR-221; ARG-225; ALA-227; GLU-231; CYS-270; HIS-270; THR-288; LEU-297; ARG-305; PHE-330 AND THR-361.
  73. "Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of false-positive newborn screening for biotinidase deficiency."
    Santer R., Gokcay G., Demirkol M., Gal A., Lukacs Z.
    J. Inherit. Metab. Dis. 28:137-140(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LPL DEFICIENCY GLU-186; GLU-215 AND THR-221.
+Additional computationally mapped references.

Entry informationi

Entry nameiLIPL_HUMAN
AccessioniPrimary (citable) accession number: P06858
Secondary accession number(s): B2R5T9
, Q16282, Q16283, Q96FC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 7, 2015
This is version 186 of the entry and version 1 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 8
    Human chromosome 8: 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

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 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.
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