UniProt ID | GPX1_MOUSE | |
---|---|---|
UniProt AC | P11352 | |
Protein Name | Glutathione peroxidase 1 | |
Gene Name | Gpx1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 201 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Protects the hemoglobin in erythrocytes from oxidative breakdown.. | |
Protein Sequence | MCAARLSAAAQSTVYAFSARPLTGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDPTALMTDPKYIIWSPVCRNDIAWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIETLLSQQSGNS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MCAARLSAAAQSTV -CCHHHHHHHHHCCE | 15.42 | 26824392 | |
12 | Phosphorylation | RLSAAAQSTVYAFSA HHHHHHHCCEEEEEC | 18.34 | - | |
23 | Phosphorylation | AFSARPLTGGEPVSL EEECCCCCCCCCCCC | 45.91 | 21082442 | |
29 | Phosphorylation | LTGGEPVSLGSLRGK CCCCCCCCCCHHCCE | 37.41 | 22817900 | |
32 | Phosphorylation | GEPVSLGSLRGKVLL CCCCCCCHHCCEEEE | 21.86 | 22324799 | |
62 | Malonylation | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | 26320211 | |
62 | Succinylation | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | 23806337 | |
62 | Glutarylation | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | 24703693 | |
62 | Acetylation | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | 23576753 | |
62 | Succinylation | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | - | |
62 | Ubiquitination | TEMNDLQKRLGPRGL HHHHHHHHHHCCCCE | 57.81 | - | |
76 | S-palmitoylation | LVVLGFPCNQFGHQE EEEEECCHHHCCCCC | 6.12 | 28526873 | |
86 | Ubiquitination | FGHQENGKNEEILNS CCCCCCCCCHHHHHH | 73.16 | - | |
86 | Succinylation | FGHQENGKNEEILNS CCCCCCCCCHHHHHH | 73.16 | 23806337 | |
86 | Malonylation | FGHQENGKNEEILNS CCCCCCCCCHHHHHH | 73.16 | 26320211 | |
86 | Acetylation | FGHQENGKNEEILNS CCCCCCCCCHHHHHH | 73.16 | 23576753 | |
86 | Succinylation | FGHQENGKNEEILNS CCCCCCCCCHHHHHH | 73.16 | - | |
93 | Phosphorylation | KNEEILNSLKYVRPG CCHHHHHHCCEECCC | 23.85 | 20469934 | |
95 | Succinylation | EEILNSLKYVRPGGG HHHHHHCCEECCCCC | 41.33 | 23806337 | |
95 | Acetylation | EEILNSLKYVRPGGG HHHHHHCCEECCCCC | 41.33 | 23864654 | |
96 | Phosphorylation | EILNSLKYVRPGGGF HHHHHCCEECCCCCC | 13.64 | 23984901 | |
112 | Succinylation | PNFTLFEKCEVNGEK CCEEEEEEEEECCEE | 28.50 | - | |
112 | Acetylation | PNFTLFEKCEVNGEK CCEEEEEEEEECCEE | 28.50 | 23576753 | |
112 | Succinylation | PNFTLFEKCEVNGEK CCEEEEEEEEECCEE | 28.50 | 23806337 | |
112 | Malonylation | PNFTLFEKCEVNGEK CCEEEEEEEEECCEE | 28.50 | 26320211 | |
119 | Acetylation | KCEVNGEKAHPLFTF EEEECCEECCHHHHH | 54.09 | 23576753 | |
119 | Ubiquitination | KCEVNGEKAHPLFTF EEEECCEECCHHHHH | 54.09 | - | |
119 | Malonylation | KCEVNGEKAHPLFTF EEEECCEECCHHHHH | 54.09 | 26320211 | |
135 | Phosphorylation | RNALPTPSDDPTALM HHCCCCCCCCCCCCC | 58.06 | 23984901 | |
139 | Phosphorylation | PTPSDDPTALMTDPK CCCCCCCCCCCCCCC | 39.14 | 29472430 | |
143 | Phosphorylation | DDPTALMTDPKYIIW CCCCCCCCCCCEEEE | 50.42 | 25195567 | |
146 | Succinylation | TALMTDPKYIIWSPV CCCCCCCCEEEECCC | 52.47 | - | |
146 | Malonylation | TALMTDPKYIIWSPV CCCCCCCCEEEECCC | 52.47 | 26073543 | |
146 | Succinylation | TALMTDPKYIIWSPV CCCCCCCCEEEECCC | 52.47 | 23806337 | |
146 | Ubiquitination | TALMTDPKYIIWSPV CCCCCCCCEEEECCC | 52.47 | - | |
146 | Acetylation | TALMTDPKYIIWSPV CCCCCCCCEEEECCC | 52.47 | 23576753 | |
147 | Phosphorylation | ALMTDPKYIIWSPVC CCCCCCCEEEECCCC | 11.74 | 25521595 | |
151 | Phosphorylation | DPKYIIWSPVCRNDI CCCEEEECCCCCCCC | 9.31 | 22942356 | |
154 | S-palmitoylation | YIIWSPVCRNDIAWN EEEECCCCCCCCCCC | 3.70 | 28526873 | |
164 | Acetylation | DIAWNFEKFLVGPDG CCCCCHHHHCCCCCC | 39.60 | 23954790 | |
195 | Phosphorylation | PDIETLLSQQSGNS- CCHHHHHHHCCCCC- | 29.32 | 23984901 | |
198 | Phosphorylation | ETLLSQQSGNS---- HHHHHHCCCCC---- | 32.10 | 22324799 | |
201 | Phosphorylation | LSQQSGNS------- HHHCCCCC------- | 45.16 | 17203969 |
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 GPX1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPX1_MOUSE !! |
* 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 GPX1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GPX1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY. |