| UniProt ID | DHRS1_MOUSE | |
|---|---|---|
| UniProt AC | Q99L04 | |
| Protein Name | Dehydrogenase/reductase SDR family member 1 | |
| Gene Name | Dhrs1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 313 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKGRLDVLVNNAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDFSSAESPEMSGKCVVALATDPNILNLSGKVLPSCDLARRYGLKDIDGRPVKDYFSLGYALSQVSSLGWLNSFLPGFLRVPKWVVTLYNSKF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Malonylation | --MVAPMKGQVCVVT --CCCCCCCCEEEEE | 45.17 | 26320211 | |
| 6 | Ubiquitination | --MVAPMKGQVCVVT --CCCCCCCCEEEEE | 45.17 | - | |
| 10 | S-nitrosocysteine | APMKGQVCVVTGASR CCCCCCEEEEECCCC | 1.24 | - | |
| 10 | S-palmitoylation | APMKGQVCVVTGASR CCCCCCEEEEECCCC | 1.24 | 28526873 | |
| 10 | S-nitrosylation | APMKGQVCVVTGASR CCCCCCEEEEECCCC | 1.24 | 21278135 | |
| 10 | Glutathionylation | APMKGQVCVVTGASR CCCCCCEEEEECCCC | 1.24 | 24333276 | |
| 21 | Methylation | GASRGIGRGIALQLC CCCCCCCHHHHHHHH | 31.27 | 24129315 | |
| 28 | S-palmitoylation | RGIALQLCKAGATVY HHHHHHHHHCCCEEE | 1.51 | 28526873 | |
| 29 | Ubiquitination | GIALQLCKAGATVYI HHHHHHHHCCCEEEE | 59.45 | - | |
| 33 | Phosphorylation | QLCKAGATVYITGRH HHHHCCCEEEEECCC | 16.96 | 29899451 | |
| 35 | Phosphorylation | CKAGATVYITGRHLD HHCCCEEEEECCCHH | 6.60 | 29899451 | |
| 47 | Phosphorylation | HLDTLRATAQEAQSL CHHHHHHHHHHHHHC | 23.57 | 29899451 | |
| 72 | Acetylation | SSQESEVKSLFEQVD CCCHHHHHHHHHHHC | 37.07 | 23201123 | |
| 83 | Acetylation | EQVDREQKGRLDVLV HHHCHHHCCCHHHHC | 41.04 | 23201123 | |
| 83 | Ubiquitination | EQVDREQKGRLDVLV HHHCHHHCCCHHHHC | 41.04 | 22790023 | |
| 130 | Glutathionylation | GLRGHYLCSVYGARL CCCCHHHHHHCCCEE | 1.72 | 24333276 | |
| 130 | S-palmitoylation | GLRGHYLCSVYGARL CCCCHHHHHHCCCEE | 1.72 | 28526873 | |
| 133 | Phosphorylation | GHYLCSVYGARLMVP CHHHHHHCCCEEEEE | 6.70 | 26032504 | |
| 177 | S-palmitoylation | CDRLAADCAHELRRH HHHHHHHHHHHHHHC | 3.41 | 28526873 | |
| 177 | S-nitrosocysteine | CDRLAADCAHELRRH HHHHHHHHHHHHHHC | 3.41 | - | |
| 177 | S-nitrosylation | CDRLAADCAHELRRH HHHHHHHHHHHHHHC | 3.41 | 21278135 | |
| 207 | Ubiquitination | MVKEFMAKEDTPEDP HHHHHHCCCCCCCCC | 44.31 | 22790023 | |
| 217 | Acetylation | TPEDPLFKKMKPDFS CCCCCHHHHCCCCCC | 60.69 | 23201123 | |
| 218 | Acetylation | PEDPLFKKMKPDFSS CCCCHHHHCCCCCCC | 44.84 | 30985811 | |
| 234 | Acetylation | ESPEMSGKCVVALAT CCCCCCCCEEEEEEC | 19.29 | 30985815 | |
| 255 | Phosphorylation | LSGKVLPSCDLARRY CCCCCCCCCHHHHHH | 18.99 | 28066266 | |
| 256 | S-palmitoylation | SGKVLPSCDLARRYG CCCCCCCCHHHHHHC | 4.73 | 28526873 | |
| 265 | Acetylation | LARRYGLKDIDGRPV HHHHHCCCCCCCCCC | 48.55 | 23201123 |
| 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 DHRS1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHRS1_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 DHRS1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DHRS1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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