CETP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CETP_HUMAN
• UniProt AC: P11597
• Protein Name: Cholesteryl ester transfer protein {ECO:0000303|PubMed:3600759}
• Gene Name: CETP {ECO:0000312|HGNC:HGNC:1869}
• Organism: Homo sapiens (Human).
• Sequence Length: 493
• Subcellular Localization: Secreted, extracellular space . Secreted in plasma.
• Protein Description: 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]
• Protein Sequence: MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITASYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESVQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
105	N-linked_Glycosylation	SIDVSIQNVSVVFKG ECCEEEEEEEEEEEC	26.76	19139490
113	Phosphorylation	VSVVFKGTLKYGYTT EEEEEECEEECCEEE	22.22	-
205	N-linked_Glycosylation	GQICKEINVISNIMA CCHHHHHHHHHHHHH	26.60	8494888
205	N-linked_Glycosylation	GQICKEINVISNIMA CCHHHHHHHHHHHHH	26.60	8494888
257	N-linked_Glycosylation	KGHFIYKNVSEDLPL CCCEEECCCCCCCCC	26.10	8494888
257	N-linked_Glycosylation	KGHFIYKNVSEDLPL CCCEEECCCCCCCCC	26.10	16335952
266	O-linked_Glycosylation	SEDLPLPTFSPTLLG CCCCCCCCCCCEECC	44.41	OGP
289	Phosphorylation	FSERVFHSLAKVAFQ HHHHHHHHHHHHHCC	20.68	26091039
349	Phosphorylation	CLKMPKISCQNKGVV EEECCCCCCCCCCEE	18.77	30622161
358	N-linked_Glycosylation	QNKGVVVNSSVMVKF CCCCEEECCEEEEEE	19.56	8494888
358	N-linked_Glycosylation	QNKGVVVNSSVMVKF CCCCEEECCEEEEEE	19.56	16335952
400	Phosphorylation	SKKKLFLSLLDFQIT CCCHHHHHHHCCCCC	21.39	24719451
407	Phosphorylation	SLLDFQITPKTVSNL HHHCCCCCHHHHHCC	14.14	24719451
413	N-linked_Glycosylation	ITPKTVSNLTESSSE CCHHHHHCCCCCCHH	46.80	8494888
413	N-linked_Glycosylation	ITPKTVSNLTESSSE CCHHHHHCCCCCCHH	46.80	8494888

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CETP_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CETP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CETP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EWS_HUMAN	EWSR1	physical	16189514
KAPCG_HUMAN	PRKACG	physical	21988832

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 143470: Hyperalphalipoproteinemia 1 (HALP1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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.
PubMed: 16335952