PON2_HUMAN - dbPTM
PON2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PON2_HUMAN
UniProt AC Q15165
Protein Name Serum paraoxonase/arylesterase 2
Gene Name PON2
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization Membrane
Peripheral membrane protein .
Protein Description Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis..
Protein Sequence MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL
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 Orthologous
Protein Cluster
81UbiquitinationLHSFAPDKPGGILMM
HHHCCCCCCCCEEEE		44.4929967540
912-HydroxyisobutyrylationGILMMDLKEEKPRAR
CEEEEECCCCCCCHH		60.61-
144UbiquitinationKNTVEIFKFEEAENS
CCEEEEEEHHHHHHH		58.4933845483
147UbiquitinationVEIFKFEEAENSLLH
EEEEEHHHHHHHCEE		65.5029967540
151PhosphorylationKFEEAENSLLHLKTV
EHHHHHHHCEEEEHH		24.6623025827
156UbiquitinationENSLLHLKTVKHELL
HHHCEEEEHHCHHHC		40.2933845483
159UbiquitinationLLHLKTVKHELLPSV
CEEEEHHCHHHCCCC		36.2729967540
220UbiquitinationKVVAEGFDSANGINI
EEEEECCCCCCCCCC		58.6629967540
227UbiquitinationDSANGINISPDDKYI
CCCCCCCCCCCCCEE		6.2922817900
232UbiquitinationINISPDDKYIYVADI
CCCCCCCCEEEHHHH		40.7129967540
243UbiquitinationVADILAHEIHVLEKH
HHHHHHHHHHHHHHC		29.2322817900
245UbiquitinationDILAHEIHVLEKHTN
HHHHHHHHHHHHCCC		18.3522817900
254N-linked_GlycosylationLEKHTNMNLTQLKVL
HHHCCCCCCCEEEEE		41.8420068230
254N-linked_GlycosylationLEKHTNMNLTQLKVL
HHHCCCCCCCEEEEE		41.8420068230
265PhosphorylationLKVLELDTLVDNLSI
EEEEEHHHCEECEEE		41.1125338102
269N-linked_GlycosylationELDTLVDNLSIDPSS
EHHHCEECEEECCCC		28.36UniProtKB CARBOHYD
277UbiquitinationLSIDPSSGDIWVGCH
EEECCCCCCEEEEEC		34.4629967540
289UbiquitinationGCHPNGQKLFVYDPN
EECCCCCEEEEECCC		45.3429967540
301UbiquitinationDPNNPPSSEVLRIQN
CCCCCCCHHHHHHHC		37.1822817900
313UbiquitinationIQNILSEKPTVTTVY
HHCHHCCCCEEEEEE		45.0222817900
323N-linked_GlycosylationVTTVYANNGSVLQGS
EEEEECCCCCEECCC		35.63UniProtKB CARBOHYD
334 (in isoform 2)Ubiquitination-21.0321906983
344PhosphorylationDGKLLIGTLYHRALY
CCEEEEEEHHHHHHH		19.7029083192
346PhosphorylationKLLIGTLYHRALYCE
EEEEEEHHHHHHHCC		6.7928152594
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 PON2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PON2_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 PON2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_HUMANRUVBL2physical
17353931
RHOA_HUMANRHOAphysical
22939629
RAP1A_HUMANRAP1Aphysical
22939629
STOM_HUMANSTOMphysical
22939629
GRP78_HUMANHSPA5physical
26186194
S39AB_HUMANSLC39A11physical
26186194
CA2D2_HUMANCACNA2D2physical
26186194
INSR_HUMANINSRphysical
26186194
SIL1_HUMANSIL1physical
26186194
LRP11_HUMANLRP11physical
26186194
NETO2_HUMANNETO2physical
26186194
CA2D1_HUMANCACNA2D1physical
26186194
IMPA3_HUMANIMPAD1physical
26186194
ENTP6_HUMANENTPD6physical
26186194
PMGT2_HUMANPOMGNT2physical
26186194
LRIG2_HUMANLRIG2physical
26186194
LRIG1_HUMANLRIG1physical
26186194
ENPP1_HUMANENPP1physical
26186194
SCRB1_HUMANSCARB1physical
26186194
SPP2B_HUMANSPPL2Bphysical
26186194
POMT2_HUMANPOMT2physical
26186194
HMR1_HUMANMR1physical
26186194
UBR2_HUMANUBR2physical
26186194
PGAP1_HUMANPGAP1physical
26186194
RDH11_HUMANRDH11physical
26186194
MOXD1_HUMANMOXD1physical
26186194
CGT_HUMANUGT8physical
26186194
MPRD_HUMANM6PRphysical
26186194
CHSTC_HUMANCHST12physical
26186194
ARSK_HUMANARSKphysical
26186194
ITA6_HUMANITGA6physical
26186194
NXPH4_HUMANNXPH4physical
26186194
EGFR_HUMANEGFRphysical
26186194
TM219_HUMANTMEM219physical
26186194
SIA10_HUMANST3GAL6physical
26186194
SAR1B_HUMANSAR1Bphysical
26186194
CHSS1_HUMANCHSY1physical
26186194
LMLN_HUMANLMLNphysical
26186194
SULF2_HUMANSULF2physical
26186194
AMGO1_HUMANAMIGO1physical
26186194
ITA4_HUMANITGA4physical
26186194
CDC6_HUMANCDC6physical
26186194
TP4A2_HUMANPTP4A2physical
26186194
GOLI_HUMANRNF130physical
26186194
ABCA2_HUMANABCA2physical
26186194
CATF_HUMANCTSFphysical
26186194
B4GT1_HUMANB4GALT1physical
26186194
LIGO1_HUMANLINGO1physical
26186194
2A5D_HUMANPPP2R5Dphysical
26186194
RN167_HUMANRNF167physical
26186194
RN170_HUMANRNF170physical
26186194
C1QL4_HUMANC1QL4physical
26186194
LRFN3_HUMANLRFN3physical
26186194
HYAL2_HUMANHYAL2physical
26186194
SMOC1_HUMANSMOC1physical
26186194
ABCA2_HUMANABCA2physical
28514442
SIA10_HUMANST3GAL6physical
28514442
CATF_HUMANCTSFphysical
28514442
AMGO1_HUMANAMIGO1physical
28514442
ARSK_HUMANARSKphysical
28514442
ITA4_HUMANITGA4physical
28514442
EGFR_HUMANEGFRphysical
28514442
CNNM1_HUMANCNNM1physical
28514442
SULF2_HUMANSULF2physical
28514442
CA2D2_HUMANCACNA2D2physical
28514442
CGT_HUMANUGT8physical
28514442
POMT2_HUMANPOMT2physical
28514442
GRP78_HUMANHSPA5physical
28514442
INSR_HUMANINSRphysical
28514442
ENTP6_HUMANENTPD6physical
28514442
ITA6_HUMANITGA6physical
28514442
LRIG2_HUMANLRIG2physical
28514442
SCRB1_HUMANSCARB1physical
28514442
TP4A2_HUMANPTP4A2physical
28514442
GOLI_HUMANRNF130physical
28514442
UBR2_HUMANUBR2physical
28514442
TM219_HUMANTMEM219physical
28514442
LMLN_HUMANLMLNphysical
28514442
SMOC1_HUMANSMOC1physical
28514442
NAR5_HUMANART5physical
28514442
PMGT2_HUMANPOMGNT2physical
28514442
LRP11_HUMANLRP11physical
28514442
NETO2_HUMANNETO2physical
28514442
ENPP1_HUMANENPP1physical
28514442
CDC6_HUMANCDC6physical
28514442
2A5D_HUMANPPP2R5Dphysical
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 PON2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-254, AND MASSSPECTROMETRY.

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