Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cholesteryl ester transfer protein  

UniProtKB / Swiss-Prot ID :  CETP_HUMAN

Gene Name (Synonyms) : 
CETP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted, extracellular space. 

Protein Function :  Involved in the transfer of insoluble cholesteryl esters in the reverse transport of cholesterol. 

Protein Sequence MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLG...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHCCCCCEECCCEEEEECHHHHHHHHHCCHHHHHHHHHCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
15A -> G (in dbSNP:rs34065661). VAR_017018
154R -> W (in dbSNP:rs34716057). VAR_033098
168L -> P (in HALP1; reduced secretion intoplasma).
299R -> C (in HALP1; reduced secretion intoplasma).
331G -> S (in dbSNP:rs5881). VAR_013919
385V -> M (in dbSNP:rs34855278). VAR_017019
390A -> P (in dbSNP:rs5880). VAR_013920
422V -> I (in dbSNP:rs5882). VAR_013921
455V -> M (in dbSNP:rs2228667). VAR_031127
459D -> G (in HALP1; dbSNP:rs2303790). VAR_004172
468R -> Q (in dbSNP:rs1800777). VAR_013922
486V -> M (in dbSNP:rs5887). VAR_013923
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
205N-linked (Glc...)CKEINVISN
HHHHHHHHH
26.60HPRD
Link
257N-linked (Glc...)FIYKNVSED
EEECCCCCC
26.10HPRD
Link
257N-linked (GlcNAc...).FIYKNVSED
EEECCCCCC
26.10UniProtKB
Link
358N-linked (Glc...)GVVVNSSVM
CEEEEEEEE
19.56HPRD
Link
358N-linked (GlcNAc...).GVVVNSSVM
CEEEEEEEE
19.56UniProtKB
Link
413N-linked (Glc...)KTVSNLTES
EHHCCCCCC
46.80HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
EWS_HUMANphysical interactionEBI-756427
intact16189514
CETP_HUMANin vitroHPRD:00325HPRD3818596
EWS_HUMANyeast 2-hybridHPRD:00325HPRD16189514
ARPC3_HUMANyeast 2-hybridHPRD:00325HPRD16169070
APOA1_HUMANENSP00000200676STRING
INS_HUMANENSP00000200676STRING
INS_HUMANENSP00000200676STRING
APOE_HUMANENSP00000200676STRING
SRBP1_HUMANENSP00000200676STRING
SRBP1_HUMANENSP00000200676STRING
SRBP1_HUMANENSP00000200676STRING
SRBP1_HUMANENSP00000200676STRING
LIPL_HUMANENSP00000200676STRING
APOA1_HUMANENSP00000200676STRING
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Disease Reference
Kegg disease
OMIM disease
143470Hyperalphalipoproteinemia 1 (HALP1)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257 AND ASN-358, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures