PRDX1_RAT - dbPTM
PRDX1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRDX1_RAT
UniProt AC Q63716
Protein Name Peroxiredoxin-1
Gene Name Prdx1
Organism Rattus norvegicus (Rat).
Sequence Length 199
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) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity)..
Protein Sequence MSSGNAKIGHPAPSFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEILRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK
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------MSSGNAKIG
------CCCCCCCCC
47.13-
7Acetylation-MSSGNAKIGHPAPS
-CCCCCCCCCCCCCC
53.90-
14PhosphorylationKIGHPAPSFKATAVM
CCCCCCCCCEEEEEC
41.2929779826
16AcetylationGHPAPSFKATAVMPD
CCCCCCCEEEEECCC
49.5222902405
18PhosphorylationPAPSFKATAVMPDGQ
CCCCCEEEEECCCCC
22.0016641100
27AcetylationVMPDGQFKDISLSDY
ECCCCCEEEEECHHC
46.3822902405
30PhosphorylationDGQFKDISLSDYKGK
CCCEEEEECHHCCCC
31.7728432305
32PhosphorylationQFKDISLSDYKGKYV
CEEEEECHHCCCCEE
31.9129779826
34PhosphorylationKDISLSDYKGKYVVF
EEEECHHCCCCEEEE
20.4716641100
35SuccinylationDISLSDYKGKYVVFF
EEECHHCCCCEEEEE
54.65-
35UbiquitinationDISLSDYKGKYVVFF
EEECHHCCCCEEEEE
54.65-
35SuccinylationDISLSDYKGKYVVFF
EEECHHCCCCEEEEE
54.65-
35AcetylationDISLSDYKGKYVVFF
EEECHHCCCCEEEEE
54.6522902405
67AcetylationSDRAEEFKKLNCQVI
CHHHHHHHHCCCEEE
60.6822902405
90PhosphorylationCHLAWINTPKKQGGL
EEEEEECCCCCCCCC
27.61-
93SuccinylationAWINTPKKQGGLGPM
EEECCCCCCCCCCCC
56.2126843850
109AcetylationIPLVSDPKRTIAQDY
CCCCCCCCCCHHHHC
68.1422902405
111PhosphorylationLVSDPKRTIAQDYGV
CCCCCCCCHHHHCCE
27.1329779826
116PhosphorylationKRTIAQDYGVLKADE
CCCHHHHCCEEECCC
9.3229779826
120AcetylationAQDYGVLKADEGISF
HHHCCEEECCCCCCE
51.9222902405
136AcetylationGLFIIDDKGILRQIT
EEEEECCCCEEEEEE
44.0722902405
152PhosphorylationNDLPVGRSVDEILRL
CCCCCCCCHHHHHHH
28.1730181290
181PhosphorylationPAGWKPGSDTIKPDV
CCCCCCCCCCCCCCC
39.8623984901
183PhosphorylationGWKPGSDTIKPDVNK
CCCCCCCCCCCCCCH
32.3723984901
185SuccinylationKPGSDTIKPDVNKSK
CCCCCCCCCCCCHHH
36.9426843850
192AcetylationKPDVNKSKEYFSKQK
CCCCCHHHHHHHCCC
59.03165087
194PhosphorylationDVNKSKEYFSKQK--
CCCHHHHHHHCCC--
19.5220178744
197AcetylationKSKEYFSKQK-----
HHHHHHHCCC-----
52.8122902405

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 PRDX1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
90TPhosphorylation

-

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 PRDX1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PRDX1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRDX1_RAT

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Related Literatures of Post-Translational Modification

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