PON1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PON1_HUMAN
• UniProt AC: P27169
• Protein Name: Serum paraoxonase/arylesterase 1 {ECO:0000303|PubMed:7916578}
• Gene Name: PON1
• Organism: Homo sapiens (Human).
• Sequence Length: 355
• Subcellular Localization: Secreted, extracellular space.
• Protein Description: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation..
• Protein Sequence: MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL

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
8	Phosphorylation	MAKLIALTLLGMGLA CHHHHHHHHHHHHHH	15.77	-
76	Phosphorylation	LKYPGIKSFNPNSPG CCCCCCCCCCCCCCC	28.47	21082442
81	Phosphorylation	IKSFNPNSPGKILLM CCCCCCCCCCEEEEE	35.97	20363803
227	N-linked_Glycosylation	FDFANGINISPDGKY CCCCCCEEECCCCCE	30.04	16335952
253	N-linked_Glycosylation	HVYEKHANWTLTPLK CEEECCCCCEECCCC	31.80	18638581
253	N-linked_Glycosylation	HVYEKHANWTLTPLK CEEECCCCCEECCCC	31.80	14760718
270	N-linked_Glycosylation	DFNTLVDNISVDPET CCCCEEECEEECCCC	22.43	UniProtKB CARBOHYD
324	N-linked_Glycosylation	VTQVYAENGTVLQGS EEEEEEECCCEECCC	43.17	17623646
324	N-linked_Glycosylation	VTQVYAENGTVLQGS EEEEEEECCCEECCC	43.17	16335952

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

Oops, there are no upstream regulatory protein records of PON1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PON1_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 PON1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NDUB6_HUMAN	NDUFB6	physical	28514442
PON3_HUMAN	PON3	physical	28514442
SFXN5_HUMAN	SFXN5	physical	28514442
RDH13_HUMAN	RDH13	physical	28514442
MICU2_HUMAN	MICU2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612633: Microvascular complications of diabetes 5 (MVCD5)
• 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

"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-253 AND ASN-324, AND MASSSPECTROMETRY.
PubMed: 19159218

"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-227; ASN-253 AND ASN-324,AND MASS SPECTROMETRY.
PubMed: 16335952

"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, AND MASSSPECTROMETRY.
PubMed: 14760718