PRDX3_HUMAN - dbPTM
PRDX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRDX3_HUMAN
UniProt AC P30048
Protein Name Thioredoxin-dependent peroxide reductase, mitochondrial
Gene Name PRDX3
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization Mitochondrion . Cytoplasm . Early endosome . Localizes to early endosomes in a RPS6KC1-dependent manner.
Protein Description Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. [PubMed: 7733872]
Protein Sequence MAAAVGRLLRASVARHVSAIPWGISATAALRPAACGRTSLTNLLCSGSSQAKLFSTSSSCHAPAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPANWTPDSPTIKPSPAASKEYFQKVNQ
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
65UbiquitinationSSCHAPAVTQHAPYF
CCCCCCCCCCCCCCC		5.29-
65AcetylationSSCHAPAVTQHAPYF
CCCCCCCCCCCCCCC		5.29-
71PhosphorylationAVTQHAPYFKGTAVV
CCCCCCCCCCCEEEE		20.7821253578
73AcetylationTQHAPYFKGTAVVNG
CCCCCCCCCEEEECC		49.89-
73SuccinylationTQHAPYFKGTAVVNG
CCCCCCCCCEEEECC		49.8923954790
73UbiquitinationTQHAPYFKGTAVVNG
CCCCCCCCCEEEECC		49.89-
73AcetylationTQHAPYFKGTAVVNG
CCCCCCCCCEEEECC		49.89-
83UbiquitinationAVVNGEFKDLSLDDF
EEECCEEECCCHHHC		54.1521890473
83SuccinylationAVVNGEFKDLSLDDF
EEECCEEECCCHHHC		54.15-
83AcetylationAVVNGEFKDLSLDDF
EEECCEEECCCHHHC		54.1523954790
83SuccinylationAVVNGEFKDLSLDDF
EEECCEEECCCHHHC		54.1527452117
86PhosphorylationNGEFKDLSLDDFKGK
CCEEECCCHHHCCCC		39.6321712546
91UbiquitinationDLSLDDFKGKYLVLF
CCCHHHCCCCEEEEE		62.5821890473
91AcetylationDLSLDDFKGKYLVLF
CCCHHHCCCCEEEEE		62.5819608861
91SuccinylationDLSLDDFKGKYLVLF
CCCHHHCCCCEEEEE		62.58-
91MalonylationDLSLDDFKGKYLVLF
CCCHHHCCCCEEEEE		62.5826320211
91SuccinylationDLSLDDFKGKYLVLF
CCCHHHCCCCEEEEE		62.58-
93AcetylationSLDDFKGKYLVLFFY
CHHHCCCCEEEEEEE		35.6830582581
131UbiquitinationDVNCEVVAVSVDSHF
CCCCEEEEEEECCCC		7.95-
146PhosphorylationSHLAWINTPRKNGGL
CEEEECCCCCCCCCC		18.4821850687
149MalonylationAWINTPRKNGGLGHM
EECCCCCCCCCCCCH		62.2326320211
149UbiquitinationAWINTPRKNGGLGHM
EECCCCCCCCCCCCH		62.2321890473
172PhosphorylationTKQISRDYGVLLEGS
HHHHHHHHCCEEECC		14.1828152594
178UbiquitinationDYGVLLEGSGLALRG
HHCCEEECCCEEEEE		27.30-
178AcetylationDYGVLLEGSGLALRG
HHCCEEECCCEEEEE		27.30-
179PhosphorylationYGVLLEGSGLALRGL
HCCEEECCCEEEEEE		22.6621712546
196SumoylationIDPNGVIKHLSVNDL
ECCCCCEEEEECCCC		35.77-
196AcetylationIDPNGVIKHLSVNDL
ECCCCCEEEEECCCC		35.7725825284
196UbiquitinationIDPNGVIKHLSVNDL
ECCCCCEEEEECCCC		35.7721890473
199PhosphorylationNGVIKHLSVNDLPVG
CCCEEEEECCCCCCC		20.7023911959
207MethylationVNDLPVGRSVEETLR
CCCCCCCCCHHHHHH		37.45115488729
214MethylationRSVEETLRLVKAFQY
CCHHHHHHHHHHHHH		44.87115488739
221PhosphorylationRLVKAFQYVETHGEV
HHHHHHHHHHHCCCC		8.1927251275
223UbiquitinationVKAFQYVETHGEVCP
HHHHHHHHHCCCCCC		30.10-
224PhosphorylationKAFQYVETHGEVCPA
HHHHHHHHCCCCCCC		25.7427251275
229S-nitrosylationVETHGEVCPANWTPD
HHHCCCCCCCCCCCC		1.9922178444
229GlutathionylationVETHGEVCPANWTPD
HHHCCCCCCCCCCCC		1.9922555962
229S-nitrosocysteineVETHGEVCPANWTPD
HHHCCCCCCCCCCCC		1.99-
230UbiquitinationETHGEVCPANWTPDS
HHCCCCCCCCCCCCC		33.53-
234PhosphorylationEVCPANWTPDSPTIK
CCCCCCCCCCCCCCC		19.6128464451
235UbiquitinationVCPANWTPDSPTIKP
CCCCCCCCCCCCCCC		31.53-
237PhosphorylationPANWTPDSPTIKPSP
CCCCCCCCCCCCCCC		25.7525159151
239PhosphorylationNWTPDSPTIKPSPAA
CCCCCCCCCCCCCHH		45.6528464451
241UbiquitinationTPDSPTIKPSPAASK
CCCCCCCCCCCHHHH		41.75-
241MalonylationTPDSPTIKPSPAASK
CCCCCCCCCCCHHHH		41.7526320211
241AcetylationTPDSPTIKPSPAASK
CCCCCCCCCCCHHHH		41.7525953088
243PhosphorylationDSPTIKPSPAASKEY
CCCCCCCCCHHHHHH		23.3625159151
247PhosphorylationIKPSPAASKEYFQKV
CCCCCHHHHHHHHHH		28.2929978859
248UbiquitinationKPSPAASKEYFQKVN
CCCCHHHHHHHHHHC		52.27-
248AcetylationKPSPAASKEYFQKVN
CCCCHHHHHHHHHHC		52.2726051181
253UbiquitinationASKEYFQKVNQ----
HHHHHHHHHCC----		33.0021890473
253AcetylationASKEYFQKVNQ----
HHHHHHHHHCC----		33.0027178108
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 PRDX3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRDX3_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 PRDX3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K13_HUMANMAP3K13physical
12492477
FANCG_HUMANFANCGphysical
17060495
RNT2_HUMANRNASET2physical
22939629
UBQL4_HUMANUBQLN4physical
22939629
PSME1_HUMANPSME1physical
22939629
TNR1A_HUMANTNFRSF1Aphysical
21988832
PRDX4_HUMANPRDX4physical
21988832
PRDX3_HUMANPRDX3physical
21988832
KS6C1_HUMANRPS6KC1physical
21988832
NUSAP_HUMANNUSAP1physical
22863883
GORS2_HUMANGORASP2physical
25416956
BIRC2_HUMANBIRC2physical
26186194
OPA1_HUMANOPA1physical
26186194
DHRS4_HUMANDHRS4physical
26186194
XIAP_HUMANXIAPphysical
26186194
BIRC2_HUMANBIRC2physical
28514442
OPA1_HUMANOPA1physical
28514442
DHRS4_HUMANDHRS4physical
28514442
XIAP_HUMANXIAPphysical
28514442
PRDX2_HUMANPRDX2physical
27173435
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 PRDX3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND MASS SPECTROMETRY.

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