PLTP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLTP_MOUSE
• UniProt AC: P55065
• Protein Name: Phospholipid transfer protein
• Gene Name: Pltp
• Organism: Mus musculus (Mouse).
• Sequence Length: 493
• Subcellular Localization: Secreted.
• Protein Description: Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer PC from phospholipid vesicles to high-density lipoproteins (HDL), and an inactive form that lacks this capability (By similarity)..
• Protein Sequence: MVLLWALFLALLAGAHAELPGCKIRVTSAALDLVKQEGLRFLEQELETITIPDVYGAKGHFYYNISDVRVTQLHLISSELHFQPDQDLLLNISNASLGLHFRRQLLYWFLYDGGYINASAEGVSIRTGLQLSQDSSGRIKVSNVSCEASVSKMNMAFGGTFRRMYNFFSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDDLVGIDYSLLKDPVVSNGNLDMEFRGAFFPLKEDNWSLPNRAVEPQLEDDERMVYVAFSEFFFDSAMESYFQAGALQLTLVGDKVPSDLDMLLRATYFGSIVLLSPTVINSPLKLKLEATSPPRCTIKPSGTTISITASVTITLAPPMLPEVELSKMIMEGRLSAKLTLRGKALRVKLDLRRFQIYSNQSALESLALIPLQAPLKTLLQIGVMPLLNERTWRGVQIPLPEGINFVREVVTNHAGFVTVGADLHFAKGLREVIDKNRPADVAASHVPPPSAAAA

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
27	Phosphorylation	PGCKIRVTSAALDLV CCCEEEEEHHHHHHH	11.64	21454597
28	Phosphorylation	GCKIRVTSAALDLVK CCEEEEEHHHHHHHH	14.53	21454597
64	N-linked_Glycosylation	AKGHFYYNISDVRVT CCCEEEEECCCCEEE	18.86	16944957
91	N-linked_Glycosylation	PDQDLLLNISNASLG CCCCEEEEECCCCCC	35.30	-
94	N-linked_Glycosylation	DLLLNISNASLGLHF CEEEEECCCCCCHHH	29.74	-
117	N-linked_Glycosylation	LYDGGYINASAEGVS HHCCCCCCEECCCEE	21.25	-
127	Phosphorylation	AEGVSIRTGLQLSQD CCCEEECCCCEECCC	40.34	22871156
135	Phosphorylation	GLQLSQDSSGRIKVS CCEECCCCCCCEEEE	27.36	22871156
143	N-linked_Glycosylation	SGRIKVSNVSCEASV CCCEEEEEEEEEEEE	32.48	-
245	N-linked_Glycosylation	FFPLKEDNWSLPNRA EEECCCCCCCCCCCC	31.18	-
330	Phosphorylation	LKLKLEATSPPRCTI EEEEEEECCCCCEEE	32.18	27087446
331	Phosphorylation	KLKLEATSPPRCTIK EEEEEECCCCCEEEC	39.70	27087446
398	N-linked_Glycosylation	RRFQIYSNQSALESL CEEECCCCHHHHHHH	23.89	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PLTP_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND MASS SPECTROMETRY.
PubMed: 16944957