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Protein

Cholesteryl ester transfer protein

Gene

CETP

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

Functioni

Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:3600759, PubMed:24293641). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (PubMed:17237796).1 Publication1 Publication1 Publication

GO - Molecular functioni

  • cholesterol binding Source: BHF-UCL
  • cholesterol transporter activity Source: UniProtKB
  • lipid binding Source: BHF-UCL
  • lipid transporter activity Source: BHF-UCL
  • phosphatidylcholine binding Source: BHF-UCL
  • phospholipid transporter activity Source: BHF-UCL
  • triglyceride binding Source: BHF-UCL

GO - Biological processi

  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: BHF-UCL
  • cholesterol transport Source: UniProtKB
  • high-density lipoprotein particle remodeling Source: UniProtKB
  • lipid homeostasis Source: BHF-UCL
  • lipid transport Source: BHF-UCL
  • lipoprotein metabolic process Source: Reactome
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • phosphatidylcholine metabolic process Source: BHF-UCL
  • phospholipid homeostasis Source: BHF-UCL
  • phospholipid transport Source: BHF-UCL
  • receptor-mediated endocytosis Source: Reactome
  • regulation of cholesterol efflux Source: BHF-UCL
  • reverse cholesterol transport Source: BHF-UCL
  • small molecule metabolic process Source: Reactome
  • triglyceride homeostasis Source: BHF-UCL
  • triglyceride metabolic process Source: BHF-UCL
  • triglyceride transport Source: UniProtKB
  • very-low-density lipoprotein particle remodeling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Enzyme and pathway databases

ReactomeiREACT_13621. HDL-mediated lipid transport.
REACT_6934. LDL-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesteryl ester transfer protein1 Publication
Alternative name(s):
Lipid transfer protein IImported
Gene namesi
Name:CETPImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1869. CETP.

Subcellular locationi

  • Secretedextracellular space 1 Publication

  • Note: Secreted in plasma.By similarity

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • high-density lipoprotein particle Source: BHF-UCL
  • vesicle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hyperalphalipoproteinemia 1 (HALP1)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels.

See also OMIM:143470
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681L → P in HALP1; reduced secretion into plasma. 1 Publication
VAR_033099
Natural varianti299 – 2991R → C in HALP1; reduced secretion into plasma. 1 Publication
VAR_033100
Natural varianti459 – 4591D → G in HALP1. 1 Publication
Corresponds to variant rs2303790 [ dbSNP | Ensembl ].
VAR_004172

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi155 – 1551T → Y: Reduces triglyceride transfer and cholesteryl ester transfer 5-fold. 1 Publication
Mutagenesisi215 – 2151V → W: Reduces triglyceride transfer 10-fold. No effect on cholesteryl ester transfer. 1 Publication
Mutagenesisi218 – 2181R → S: Reduces triglyceride transfer 10-fold. Slight reduction of cholesteryl ester transfer. 1 Publication
Mutagenesisi247 – 2471S → A: Reduces triglyceride transfer 5-fold. Slight reduction of cholesteryl ester transfer. 1 Publication
Mutagenesisi282 – 2821F → R: Not secreted. 1 Publication
Mutagenesisi287 – 2871F → R: Not secreted. 1 Publication
Mutagenesisi309 – 3091F → D: Not secreted. 1 Publication
Mutagenesisi313 – 3131L → Q: Reduces cholesteryl ester transfer by 60%. 1 Publication
Mutagenesisi392 – 3921Y → S: Not secreted. 1 Publication
Mutagenesisi399 – 3991L → W: Not secreted. 1 Publication
Mutagenesisi433 – 4331V → R: Reduces activity by 60%. 1 Publication

Keywords - Diseasei

Atherosclerosis, Disease mutation

Organism-specific databases

MIMi143470. phenotype.
Orphaneti79506. Cholesterol-ester transfer protein deficiency.
PharmGKBiPA108.

Polymorphism and mutation databases

BioMutaiCETP.
DMDMi71153497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 493476Cholesteryl ester transfer proteinPRO_0000017155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi105 – 1051N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi160 ↔ 2011 Publication
Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
Glycosylationi358 – 3581N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP11597.
PeptideAtlasiP11597.
PRIDEiP11597.

PTM databases

PhosphoSiteiP11597.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP11597.
CleanExiHS_CETP.
ExpressionAtlasiP11597. baseline and differential.
GenevisibleiP11597. HS.

Interactioni

Protein-protein interaction databases

BioGridi107498. 2 interactions.
IntActiP11597. 3 interactions.
STRINGi9606.ENSP00000200676.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 337Combined sources
Helixi34 – 407Combined sources
Helixi41 – 433Combined sources
Helixi44 – 5411Combined sources
Beta strandi60 – 667Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 9425Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 12023Combined sources
Helixi122 – 1243Combined sources
Beta strandi128 – 14922Combined sources
Beta strandi152 – 17120Combined sources
Helixi172 – 1743Combined sources
Helixi180 – 1878Combined sources
Helixi189 – 22234Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi242 – 2498Combined sources
Beta strandi252 – 2554Combined sources
Helixi269 – 2713Combined sources
Beta strandi274 – 28310Combined sources
Helixi284 – 29613Combined sources
Beta strandi300 – 3045Combined sources
Helixi306 – 31510Combined sources
Helixi323 – 3253Combined sources
Helixi326 – 3294Combined sources
Helixi333 – 3353Combined sources
Beta strandi337 – 3448Combined sources
Beta strandi347 – 3515Combined sources
Beta strandi354 – 36714Combined sources
Helixi372 – 3743Combined sources
Beta strandi378 – 39316Combined sources
Beta strandi396 – 41621Combined sources
Helixi420 – 43213Combined sources
Helixi434 – 45118Combined sources
Turni452 – 4543Combined sources
Helixi455 – 4573Combined sources
Beta strandi458 – 46811Combined sources
Beta strandi471 – 4799Combined sources
Helixi482 – 4909Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OBDX-ray2.10A18-493[»]
4EWSX-ray2.59A18-493[»]
4F2AX-ray3.11A18-493[»]
ProteinModelPortaliP11597.
SMRiP11597. Positions 22-493.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11597.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG252260.
GeneTreeiENSGT00390000008226.
HOGENOMiHOG000111553.
HOVERGENiHBG005310.
InParanoidiP11597.
KOiK16835.
OMAiPKISCQN.
OrthoDBiEOG783MV4.
PhylomeDBiP11597.
TreeFamiTF333484.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR017130. Cholesteryl_ester_transfer.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504:SF12. PTHR10504:SF12. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF037185. Cholesteryl_ester_transf. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11597-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MLAATVLTLA LLGNAHACSK GTSHEAGIVC RITKPALLVL NHETAKVIQT
60 70 80 90 100
AFQRASYPDI TGEKAMMLLG QVKYGLHNIQ ISHLSIASSQ VELVEAKSID
110 120 130 140 150
VSIQNVSVVF KGTLKYGYTT AWWLGIDQSI DFEIDSAIDL QINTQLTCDS
160 170 180 190 200
GRVRTDAPDC YLSFHKLLLH LQGEREPGWI KQLFTNFISF TLKLVLKGQI
210 220 230 240 250
CKEINVISNI MADFVQTRAA SILSDGDIGV DISLTGDPVI TASYLESHHK
260 270 280 290 300
GHFIYKNVSE DLPLPTFSPT LLGDSRMLYF WFSERVFHSL AKVAFQDGRL
310 320 330 340 350
MLSLMGDEFK AVLETWGFNT NQEIFQEVVG GFPSQAQVTV HCLKMPKISC
360 370 380 390 400
QNKGVVVNSS VMVKFLFPRP DQQHSVAYTF EEDIVTTVQA SYSKKKLFLS
410 420 430 440 450
LLDFQITPKT VSNLTESSSE SVQSFLQSMI TAVGIPEVMS RLEVVFTALM
460 470 480 490
NSKGVSLFDI INPEIITRDG FLLLQMDFGF PEHLLVDFLQ SLS
Length:493
Mass (Da):54,756
Last modified:July 19, 2005 - v2
Checksum:iCD7762766A9B062E
GO
Isoform 2 (identifier: P11597-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     251-310: Missing.

Show »
Length:433
Mass (Da):47,787
Checksum:iED675FD1456F78F7
GO

Polymorphismi

Genetic variations in CETP define the high density lipoprotein cholesterol level quantitative trait locus 10 (HDLCQ10) [MIMi:143470].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151A → G.1 Publication
Corresponds to variant rs34065661 [ dbSNP | Ensembl ].
VAR_017018
Natural varianti154 – 1541R → W.
Corresponds to variant rs34716057 [ dbSNP | Ensembl ].
VAR_033098
Natural varianti168 – 1681L → P in HALP1; reduced secretion into plasma. 1 Publication
VAR_033099
Natural varianti299 – 2991R → C in HALP1; reduced secretion into plasma. 1 Publication
VAR_033100
Natural varianti331 – 3311G → S.1 Publication
Corresponds to variant rs5881 [ dbSNP | Ensembl ].
VAR_013919
Natural varianti385 – 3851V → M.1 Publication
Corresponds to variant rs34855278 [ dbSNP | Ensembl ].
VAR_017019
Natural varianti390 – 3901A → P.2 Publications
Corresponds to variant rs5880 [ dbSNP | Ensembl ].
VAR_013920
Natural varianti422 – 4221V → I.6 Publications
Corresponds to variant rs5882 [ dbSNP | Ensembl ].
VAR_013921
Natural varianti455 – 4551V → M.
Corresponds to variant rs2228667 [ dbSNP | Ensembl ].
VAR_031127
Natural varianti459 – 4591D → G in HALP1. 1 Publication
Corresponds to variant rs2303790 [ dbSNP | Ensembl ].
VAR_004172
Natural varianti468 – 4681R → Q.1 Publication
Corresponds to variant rs1800777 [ dbSNP | Ensembl ].
VAR_013922
Natural varianti486 – 4861V → M.1 Publication
Corresponds to variant rs5887 [ dbSNP | Ensembl ].
VAR_013923

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei251 – 31060Missing in isoform 2. 1 PublicationVSP_023645Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30185 mRNA. Translation: AAA51977.1.
M32998
, M32992, M32993, M32994, M32995, M32996, M32997 Genomic DNA. Translation: AAA51978.1.
AY422211 Genomic DNA. Translation: AAR03500.1.
BC025739 mRNA. Translation: AAH25739.1.
U71187 Genomic DNA. Translation: AAD14876.1.
AF027656 Genomic DNA. Translation: AAB86604.1.
M83573 mRNA. Translation: AAB59388.1.
CCDSiCCDS10772.1. [P11597-1]
CCDS67032.1. [P11597-2]
PIRiA26941.
RefSeqiNP_000069.2. NM_000078.2. [P11597-1]
UniGeneiHs.89538.

Genome annotation databases

EnsembliENST00000200676; ENSP00000200676; ENSG00000087237.
ENST00000379780; ENSP00000369106; ENSG00000087237. [P11597-2]
GeneIDi1071.
KEGGihsa:1071.
UCSCiuc002eki.2. human. [P11597-1]
uc002ekj.2. human. [P11597-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Cholesterylester transfer protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30185 mRNA. Translation: AAA51977.1.
M32998
, M32992, M32993, M32994, M32995, M32996, M32997 Genomic DNA. Translation: AAA51978.1.
AY422211 Genomic DNA. Translation: AAR03500.1.
BC025739 mRNA. Translation: AAH25739.1.
U71187 Genomic DNA. Translation: AAD14876.1.
AF027656 Genomic DNA. Translation: AAB86604.1.
M83573 mRNA. Translation: AAB59388.1.
CCDSiCCDS10772.1. [P11597-1]
CCDS67032.1. [P11597-2]
PIRiA26941.
RefSeqiNP_000069.2. NM_000078.2. [P11597-1]
UniGeneiHs.89538.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OBDX-ray2.10A18-493[»]
4EWSX-ray2.59A18-493[»]
4F2AX-ray3.11A18-493[»]
ProteinModelPortaliP11597.
SMRiP11597. Positions 22-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107498. 2 interactions.
IntActiP11597. 3 interactions.
STRINGi9606.ENSP00000200676.

Chemistry

BindingDBiP11597.
ChEMBLiCHEMBL3572.

PTM databases

PhosphoSiteiP11597.

Polymorphism and mutation databases

BioMutaiCETP.
DMDMi71153497.

Proteomic databases

PaxDbiP11597.
PeptideAtlasiP11597.
PRIDEiP11597.

Protocols and materials databases

DNASUi1071.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000200676; ENSP00000200676; ENSG00000087237.
ENST00000379780; ENSP00000369106; ENSG00000087237. [P11597-2]
GeneIDi1071.
KEGGihsa:1071.
UCSCiuc002eki.2. human. [P11597-1]
uc002ekj.2. human. [P11597-2]

Organism-specific databases

CTDi1071.
GeneCardsiGC16P056996.
HGNCiHGNC:1869. CETP.
MIMi118470. gene.
143470. phenotype.
neXtProtiNX_P11597.
Orphaneti79506. Cholesterol-ester transfer protein deficiency.
PharmGKBiPA108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252260.
GeneTreeiENSGT00390000008226.
HOGENOMiHOG000111553.
HOVERGENiHBG005310.
InParanoidiP11597.
KOiK16835.
OMAiPKISCQN.
OrthoDBiEOG783MV4.
PhylomeDBiP11597.
TreeFamiTF333484.

Enzyme and pathway databases

ReactomeiREACT_13621. HDL-mediated lipid transport.
REACT_6934. LDL-mediated lipid transport.

Miscellaneous databases

EvolutionaryTraceiP11597.
GeneWikiiCholesterylester_transfer_protein.
GenomeRNAii1071.
NextBioi4472.
PROiP11597.
SOURCEiSearch...

Gene expression databases

BgeeiP11597.
CleanExiHS_CETP.
ExpressionAtlasiP11597. baseline and differential.
GenevisibleiP11597. HS.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR017130. Cholesteryl_ester_transfer.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504:SF12. PTHR10504:SF12. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF037185. Cholesteryl_ester_transf. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of human cholesteryl ester transfer protein cDNA."
    Drayna D., Jarnagin A.S., McLean J., Henzel W., Kohr W., Fielding C., Lawn R.
    Nature 327:632-634(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, VARIANT ILE-422.
  2. "Organization of the human cholesteryl ester transfer protein gene."
    Agellon L.B., Quinet E.M., Gillette T.G., Drayna D.T., Brown M.L., Tall A.R.
    Biochemistry 29:1372-1376(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Nickerson D.A.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-422.
  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), VARIANT ILE-422.
    Tissue: Pancreas and Spleen.
  5. "Human cholesteryl ester transfer protein gene proximal promoter contains dietary cholesterol positive responsive elements and mediates expression in small intestine and periphery while predominant liver and spleen expression is controlled by 5'-distal sequences. Cis-acting sequences mapped in transgenic mice."
    Oliveira C.F.O., Chouinard R.A., Agellon L.B., Bruce C., Ma L., Walsh A., Breslow J.L., Tall A.R.
    J. Biol. Chem. 271:31831-31838(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
  6. "Sequencing of the cholesteryl ester transfer protein 5' regulatory region using artificial transposons."
    Williams S., Hayes L., Elsenboss L., Williams A., Andre C., Abramson R., Thompson J.F., Milos P.M.
    Gene 197:101-107(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
  7. Dinchuk J.E., Hart J.T., Wirak D.O.
    Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-493 (ISOFORM 2), VARIANT ILE-422.
    Tissue: Liver.
  8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257 AND ASN-358.
    Tissue: Plasma.
  9. Cited for: GLYCOSYLATION AT ASN-105.
  10. "Cholesteryl ester transfer proteins from different species do not have equivalent activities."
    Morton R.E., Izem L.
    J. Lipid Res. 55:258-265(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-493 IN COMPLEX WITH LIPID, FUNCTION, DISULFIDE BOND, MUTAGENESIS OF THR-155; VAL-215; ARG-218; SER-247; PHE-282; PHE-287; PHE-309; LEU-313; TYR-392; LEU-399 AND VAL-433.
  12. "Increased high-density lipoprotein levels caused by a common cholesteryl-ester transfer protein gene mutation."
    Inazu A., Brown M.L., Hesler C.B., Agellon L.B., Koizumi J., Takata K., Maruhama Y., Mabuchi H., Tall A.R.
    N. Engl. J. Med. 323:1234-1238(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HALP1.
  13. "A missense mutation in the cholesteryl ester transfer protein gene with possible dominant effects on plasma high density lipoproteins."
    Takahashi K., Jiang X.-C., Sakai N., Yamashita S., Hirano K., Bujo H., Yamazaki H., Kusunoki J., Miura T., Kussie P., Matsuzawa Y., Saito Y., Tall A.
    J. Clin. Invest. 92:2060-2064(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HALP1 GLY-459.
  14. Cited for: VARIANTS SER-331; PRO-390; ILE-422 AND MET-486.
  15. "Two novel missense mutations in the CETP gene in Japanese hyperalphalipoproteinemic subjects: high-throughput assay by Invader assay."
    Nagano M., Yamashita S., Hirano K., Ito M., Maruyama T., Ishihara M., Sagehashi Y., Oka T., Kujiraoka T., Hattori H., Nakajima N., Egashira T., Kondo M., Sakai N., Matsuzawa Y.
    J. Lipid Res. 43:1011-1018(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HALP1 PRO-168 AND CYS-299, CHARACTERIZATION OF VARIANTS HALP1 PRO-168 AND CYS-299.
  16. "Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
    Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
    Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-15; MET-385; PRO-390; ILE-422 AND GLN-468.

Entry informationi

Entry nameiCETP_HUMAN
AccessioniPrimary (citable) accession number: P11597
Secondary accession number(s): Q13987, Q13988, Q53YZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 19, 2005
Last modified: July 22, 2015
This is version 163 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.