PON3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PON3_HUMAN
• UniProt AC: Q15166
• Protein Name: Serum paraoxonase/lactonase 3
• Gene Name: PON3
• Organism: Homo sapiens (Human).
• Sequence Length: 354
• Subcellular Localization: Secreted, extracellular space.
• Protein Description: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents..
• Protein Sequence: MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFIDKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYATRDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVAAKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL

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
15	Phosphorylation	VLLGVGLSLVGEMFL HHHHHHHHHHHHHHH	18.32	-
29	N-linked_Glycosylation	LAFRERVNASREVEP HHHHHHHCCCCCCCC	38.12	UniProtKB CARBOHYD
117	Phosphorylation	LFNPHGISIFIDKDN HCCCCEEEEEECCCC	18.95	18452278
165	Phosphorylation	IKHELLKSVNDIVVL HHHHHHHCCCEEEEE	26.56	22817900
178	Phosphorylation	VLGPEQFYATRDHYF EECHHHHCCCCCHHH	13.52	19690332
184	Phosphorylation	FYATRDHYFTNSLLS HCCCCCHHHHHHHHH	19.18	22210691
188	Phosphorylation	RDHYFTNSLLSFFEM CCHHHHHHHHHHHHH	27.85	22210691
191	Phosphorylation	YFTNSLLSFFEMILD HHHHHHHHHHHHHHH	32.93	22210691
202	Phosphorylation	MILDLRWTYVLFYSP HHHHHCCEEEEEECC	9.41	29759185
203	Phosphorylation	ILDLRWTYVLFYSPR HHHHCCEEEEEECCC	6.54	29759185
207	Phosphorylation	RWTYVLFYSPREVKV CCEEEEEECCCEEEE	17.38	29759185
208	Phosphorylation	WTYVLFYSPREVKVV CEEEEEECCCEEEEE	15.33	29759185
269	N-linked_Glycosylation	QLGTLVDNLTVDPAT ECCCEECCEEECCCC	30.08	UniProtKB CARBOHYD
313	Ubiquitination	IQNVLSEKPRVSTVY EEECCCCCCCEEEEE	34.45	33845483
323	N-linked_Glycosylation	VSTVYANNGSVLQGT EEEEECCCCCEECCC	35.63	16335952
325	Phosphorylation	TVYANNGSVLQGTSV EEECCCCCEECCCEE	23.06	19702290
336	Phosphorylation	GTSVASVYHGKILIG CCEEEEEECCEEEEE	11.45	-

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

Oops, there are no upstream regulatory protein records of PON3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PON3_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 PON3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PON3_HUMAN !!

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.

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-323, AND MASSSPECTROMETRY.
PubMed: 16335952

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
PubMed: 19690332