PRDX2_HUMAN - dbPTM
PRDX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRDX2_HUMAN
UniProt AC P32119
Protein Name Peroxiredoxin-2
Gene Name PRDX2
Organism Homo sapiens (Human).
Sequence Length 198
Subcellular Localization Cytoplasm .
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 and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2)..
Protein Sequence MASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSNRAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKHN
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
2Acetylation------MASGNARIG
------CCCCCCCCC		26.5819413330
3Phosphorylation-----MASGNARIGK
-----CCCCCCCCCC		31.14-
10UbiquitinationSGNARIGKPAPDFKA
CCCCCCCCCCCCCCE		35.32-
10AcetylationSGNARIGKPAPDFKA
CCCCCCCCCCCCCCE		35.3226051181
10MalonylationSGNARIGKPAPDFKA
CCCCCCCCCCCCCCE		35.3226320211
16UbiquitinationGKPAPDFKATAVVDG
CCCCCCCCEEEEEEC		52.8121890473
16AcetylationGKPAPDFKATAVVDG
CCCCCCCCEEEEEEC		52.8125953088
16UbiquitinationGKPAPDFKATAVVDG
CCCCCCCCEEEEEEC		52.8121906983
18PhosphorylationPAPDFKATAVVDGAF
CCCCCCEEEEEECCE		22.1521712546
18O-linked_GlycosylationPAPDFKATAVVDGAF
CCCCCCEEEEEECCE		22.1563769329
26UbiquitinationAVVDGAFKEVKLSDY
EEEECCEEEEECHHC		62.1521890473
26AcetylationAVVDGAFKEVKLSDY
EEEECCEEEEECHHC		62.1523954790
26SuccinylationAVVDGAFKEVKLSDY
EEEECCEEEEECHHC		62.1523954790
26UbiquitinationAVVDGAFKEVKLSDY
EEEECCEEEEECHHC		62.1521890473
29AcetylationDGAFKEVKLSDYKGK
ECCEEEEECHHCCCC		43.2825953088
29UbiquitinationDGAFKEVKLSDYKGK
ECCEEEEECHHCCCC		43.28-
31PhosphorylationAFKEVKLSDYKGKYV
CEEEEECHHCCCCEE		32.9323312004
33PhosphorylationKEVKLSDYKGKYVVL
EEEECHHCCCCEEEE		20.4723312004
33NitrationKEVKLSDYKGKYVVL
EEEECHHCCCCEEEE		20.47-
34AcetylationEVKLSDYKGKYVVLF
EEECHHCCCCEEEEE		54.6526051181
76PhosphorylationGCEVLGVSVDSQFTH
CCEEECCEECCCCCE		20.5722210691
82PhosphorylationVSVDSQFTHLAWINT
CEECCCCCEEEEECC		14.3522210691
89PhosphorylationTHLAWINTPRKEGGL
CEEEEECCCCCCCCC		18.4817610816
92UbiquitinationAWINTPRKEGGLGPL
EEECCCCCCCCCCCC		63.0121890473
108PhosphorylationIPLLADVTRRLSEDY
HHHHHHHHHHHHHHC		15.60-
110MethylationLLADVTRRLSEDYGV
HHHHHHHHHHHHCCE		32.95115488705
112O-linked_GlycosylationADVTRRLSEDYGVLK
HHHHHHHHHHCCEEE		26.9826374642
112PhosphorylationADVTRRLSEDYGVLK
HHHHHHHHHHCCEEE		26.9821712546
115PhosphorylationTRRLSEDYGVLKTDE
HHHHHHHCCEEECCC		12.7028796482
119SuccinylationSEDYGVLKTDEGIAY
HHHCCEEECCCCCEE		52.0723954790
119UbiquitinationSEDYGVLKTDEGIAY
HHHCCEEECCCCCEE		52.0721890473
119AcetylationSEDYGVLKTDEGIAY
HHHCCEEECCCCCEE		52.0723954790
120PhosphorylationEDYGVLKTDEGIAYR
HHCCEEECCCCCEEE		34.8128857561
126PhosphorylationKTDEGIAYRGLFIID
ECCCCCEEEEEEEEC		11.86-
126NitrationKTDEGIAYRGLFIID
ECCCCCEEEEEEEEC		11.86-
127MethylationTDEGIAYRGLFIIDG
CCCCCEEEEEEEECC		26.73115488721
128 (in isoform 2)Phosphorylation-16.56-
135UbiquitinationGLFIIDGKGVLRQIT
EEEEECCCCEEEEEE		41.9421890473
135AcetylationGLFIIDGKGVLRQIT
EEEEECCCCEEEEEE		41.9426051181
135SuccinylationGLFIIDGKGVLRQIT
EEEEECCCCEEEEEE		41.9423954790
142PhosphorylationKGVLRQITVNDLPVG
CCEEEEEEECCCCCC		12.6228450419
150MethylationVNDLPVGRSVDEALR
ECCCCCCCCHHHHHH		33.47-
151PhosphorylationNDLPVGRSVDEALRL
CCCCCCCCHHHHHHH		28.1730624053
157MethylationRSVDEALRLVQAFQY
CCHHHHHHHHHHHHC		39.60115488713
177UbiquitinationEVCPAGWKPGSDTIK
CCCCCCCCCCCCCCC		38.29-
177AcetylationEVCPAGWKPGSDTIK
CCCCCCCCCCCCCCC		38.2923749302
177MethylationEVCPAGWKPGSDTIK
CCCCCCCCCCCCCCC		38.29-
180PhosphorylationPAGWKPGSDTIKPNV
CCCCCCCCCCCCCCC		39.8624275569
182PhosphorylationGWKPGSDTIKPNVDD
CCCCCCCCCCCCCCC		32.3714702039
184AcetylationKPGSDTIKPNVDDSK
CCCCCCCCCCCCCHH		32.4127452117
190PhosphorylationIKPNVDDSKEYFSKH
CCCCCCCHHHHHHHC		23.9528152594
191SumoylationKPNVDDSKEYFSKHN
CCCCCCHHHHHHHCC		64.53-
191SumoylationKPNVDDSKEYFSKHN
CCCCCCHHHHHHHCC		64.53-
191MalonylationKPNVDDSKEYFSKHN
CCCCCCHHHHHHHCC		64.5326320211
191AcetylationKPNVDDSKEYFSKHN
CCCCCCHHHHHHHCC		64.5326051181
191UbiquitinationKPNVDDSKEYFSKHN
CCCCCCHHHHHHHCC		64.53-
193PhosphorylationNVDDSKEYFSKHN--
CCCCHHHHHHHCC--		19.5227273156
193NitrationNVDDSKEYFSKHN--
CCCCHHHHHHHCC--		19.52-
195PhosphorylationDDSKEYFSKHN----
CCHHHHHHHCC----		31.9128152594
196AcetylationDSKEYFSKHN-----
CHHHHHHHCC-----		36.9518606987
196SuccinylationDSKEYFSKHN-----
CHHHHHHHCC-----		36.9523954790
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 PRDX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRDX2_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 PRDX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
URM1_HUMANURM1physical
22939629
PRDX5_HUMANPRDX5physical
22939629
SPHM_HUMANSGSHphysical
22939629
UBA3_HUMANUBA3physical
22939629
TIPRL_HUMANTIPRLphysical
22939629
TMEM9_HUMANTMEM9physical
22939629
RIF1_HUMANRIF1physical
22939629
S23IP_HUMANSEC23IPphysical
22939629
PRDX6_HUMANPRDX6physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
UBE2H_HUMANUBE2Hphysical
22939629
SODC_HUMANSOD1physical
22939629
SAT1_HUMANSAT1physical
21988832
UTY_HUMANUTYphysical
21988832
1433Z_HUMANYWHAZphysical
21988832
PRDX4_HUMANPRDX4physical
21988832
PRDX1_HUMANPRDX1physical
22863883
ANXA2_HUMANANXA2physical
26344197
DUT_HUMANDUTphysical
26344197
MSH6_HUMANMSH6physical
26344197
PCBP1_HUMANPCBP1physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PRDX3_HUMANPRDX3physical
26344197
TALDO_HUMANTALDO1physical
26344197
TPIS_HUMANTPI1physical
26344197
COEA1_HUMANCOL14A1physical
27173435
RTL9_HUMANRGAG1physical
27173435
KCTD5_HUMANKCTD5physical
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 PRDX2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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