dbPTM

PLTP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLTP_HUMAN
UniProt AC	P55058
Protein Name	Phospholipid transfer protein
Gene Name	PLTP
Organism	Homo sapiens (Human).
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..
Protein Sequence	MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGHFYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASAEGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFPLTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLDMLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQPEVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQIGVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADVRASTAPTPSTAAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	O-linked_Glycosylation	GCKIRVTSKALELVK CCEEEEEHHHHHHHH	17.05	31637018
64	N-linked_Glycosylation	KEGHFYYNISEVKVT CCCEEEEEECEEEEE	21.67	17623646
64	N-linked_Glycosylation	KEGHFYYNISEVKVT CCCEEEEEECEEEEE	21.67	17623646
93	Phosphorylation	QELMLQITNASLGLR HHHHHHHHHHHHHHH	16.27	18669648
94	N-linked_Glycosylation	ELMLQITNASLGLRF HHHHHHHHHHHHHHH	29.21	16335952
96	Phosphorylation	MLQITNASLGLRFRR HHHHHHHHHHHHHHH	25.66	18669648
117	N-linked_Glycosylation	FYDGGYINASAEGVS ECCCCEEEEECCCEE	21.25	21515415
143	N-linked_Glycosylation	AGRMKVSNVSCQASV CCCCEECCCEECCCH	32.48	18638581
165	Phosphorylation	GGTFKKVYDFLSTFI CCHHHHHHHHHHHHH	15.17	25072903
169	Phosphorylation	KKVYDFLSTFITSGM HHHHHHHHHHHHHHH	22.67	25072903
170	Phosphorylation	KVYDFLSTFITSGMR HHHHHHHHHHHHHHH	22.62	25072903
173	Phosphorylation	DFLSTFITSGMRFLL HHHHHHHHHHHHHHH	18.29	25072903
174	Phosphorylation	FLSTFITSGMRFLLN HHHHHHHHHHHHHHH	26.27	25072903
245	N-linked_Glycosylation	FFPLTERNWSLPNRA CCCCCCCCCCCCCCC	26.84	19139490
376	Ubiquitination	MDARLSAKMALRGKA HHHHHHHHHHHCCHH	22.72	-
398	N-linked_Glycosylation	RRFRIYSNHSALESL HHHCCCCCCCHHHHH	19.03	16335952
398	N-linked_Glycosylation	RRFRIYSNHSALESL HHHCCCCCCCHHHHH	19.03	17623646
483	O-linked_Glycosylation	RPADVRASTAPTPST CCCCCCCCCCCCCCC	17.97	55833439
484	O-linked_Glycosylation	PADVRASTAPTPSTA CCCCCCCCCCCCCCC	35.35	55833445
487	O-linked_Glycosylation	VRASTAPTPSTAAV- CCCCCCCCCCCCCC-	27.66	55833449
489	O-linked_Glycosylation	ASTAPTPSTAAV--- CCCCCCCCCCCC---	32.91	55833453
490	O-linked_Glycosylation	STAPTPSTAAV---- CCCCCCCCCCC----	21.60	55833459

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of PLTP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PLTP_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PLTP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APOA1_HUMAN	APOA1	physical	9469594
APOA2_HUMAN	APOA2	physical	9469594
CLGN_HUMAN	CLGN	physical	26186194
CALX_HUMAN	CANX	physical	26186194
HLAF_HUMAN	HLA-F	physical	26186194
IPRI_HUMAN	ITPRIP	physical	26186194
RDH11_HUMAN	RDH11	physical	26186194
CGT_HUMAN	UGT8	physical	26186194
PTN1_HUMAN	PTPN1	physical	26186194
E41L5_HUMAN	EPB41L5	physical	26186194
ADPGK_HUMAN	ADPGK	physical	26186194
PCYOX_HUMAN	PCYOX1	physical	26186194
GLBL2_HUMAN	GLB1L2	physical	26186194
PGAP1_HUMAN	PGAP1	physical	26186194
RAP1B_HUMAN	RAP1B	physical	26186194
IMPA3_HUMAN	IMPAD1	physical	26186194
FA69A_HUMAN	FAM69A	physical	26186194
GPC6_HUMAN	GPC6	physical	26186194
DYR2_HUMAN	DHFRL1	physical	26186194
SE1L3_HUMAN	SEL1L3	physical	26186194
NMD3_HUMAN	NMD3	physical	26186194
GALT7_HUMAN	GALNT7	physical	26186194
SE1L3_HUMAN	SEL1L3	physical	28514442
CGT_HUMAN	UGT8	physical	28514442
E41L5_HUMAN	EPB41L5	physical	28514442
DYR2_HUMAN	DHFRL1	physical	28514442
ADPGK_HUMAN	ADPGK	physical	28514442
FUT10_HUMAN	FUT10	physical	28514442
CALX_HUMAN	CANX	physical	28514442
IMPA3_HUMAN	IMPAD1	physical	28514442
GLBL2_HUMAN	GLB1L2	physical	28514442
FA69A_HUMAN	FAM69A	physical	28514442
RAP1B_HUMAN	RAP1B	physical	28514442
IPRI_HUMAN	ITPRIP	physical	28514442
GALT7_HUMAN	GALNT7	physical	28514442

Drug and Disease Associations

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

Regulatory Network of PLTP_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND MASS SPECTROMETRY.	19159218 [Abstract]
"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-64; ASN-94; ASN-143;ASN-245 AND ASN-398, AND MASS SPECTROMETRY.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93 AND SER-96, AND MASSSPECTROMETRY.	18669648 [Abstract]