| UniProt ID | DHB11_HUMAN | |
|---|---|---|
| UniProt AC | Q8NBQ5 | |
| Protein Name | Estradiol 17-beta-dehydrogenase 11 | |
| Gene Name | HSD17B11 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 300 | |
| Subcellular Localization | Secreted . | |
| Protein Description | Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell lymphoma.. | |
| Protein Sequence | MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLKSKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKVKAEIGDVSILVNNAGVVYTSDLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMTKNNHGHIVTVASAAGHVSVPFLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPEEVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKQKISVKFDAVIGYKMKAQ | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MKFLLDILL ------CHHHHHHHH | 44.73 | 20167786 | |
| 33 | Phosphorylation | FIPKRRKSVTGEIVL HCCCCCCCCCCCEEE | 24.09 | 26657352 | |
| 35 | Phosphorylation | PKRRKSVTGEIVLIT CCCCCCCCCCEEEEC | 35.87 | 28450419 | |
| 42 | Phosphorylation | TGEIVLITGAGHGIG CCCEEEECCCCCCHH | 19.47 | 28102081 | |
| 58 | Ubiquitination | LTAYEFAKLKSKLVL HHHHHHHHHHCEEEE | 62.86 | 33845483 | |
| 60 | Trimethylation | AYEFAKLKSKLVLWD HHHHHHHHCEEEEEE | 44.85 | - | |
| 60 | Methylation | AYEFAKLKSKLVLWD HHHHHHHHCEEEEEE | 44.85 | - | |
| 60 | Ubiquitination | AYEFAKLKSKLVLWD HHHHHHHHCEEEEEE | 44.85 | 22817900 | |
| 62 | Trimethylation | EFAKLKSKLVLWDIN HHHHHHCEEEEEECH | 40.82 | - | |
| 62 | Ubiquitination | EFAKLKSKLVLWDIN HHHHHHCEEEEEECH | 40.82 | 21890473 | |
| 62 | Methylation | EFAKLKSKLVLWDIN HHHHHHCEEEEEECH | 40.82 | - | |
| 62 | Acetylation | EFAKLKSKLVLWDIN HHHHHHCEEEEEECH | 40.82 | 25953088 | |
| 62 | Malonylation | EFAKLKSKLVLWDIN HHHHHHCEEEEEECH | 40.82 | 26320211 | |
| 70 | Methylation | LVLWDINKHGLEETA EEEEECHHCCHHHHH | 39.11 | - | |
| 70 | Malonylation | LVLWDINKHGLEETA EEEEECHHCCHHHHH | 39.11 | 26320211 | |
| 70 | Acetylation | LVLWDINKHGLEETA EEEEECHHCCHHHHH | 39.11 | 23236377 | |
| 70 | Trimethylation | LVLWDINKHGLEETA EEEEECHHCCHHHHH | 39.11 | - | |
| 70 | Ubiquitination | LVLWDINKHGLEETA EEEEECHHCCHHHHH | 39.11 | 21906983 | |
| 79 | Ubiquitination | GLEETAAKCKGLGAK CHHHHHHHCCCCCCE | 33.73 | 29967540 | |
| 86 | Malonylation | KCKGLGAKVHTFVVD HCCCCCCEEEEEEEE | 32.52 | 26320211 | |
| 86 | Ubiquitination | KCKGLGAKVHTFVVD HCCCCCCEEEEEEEE | 32.52 | 29967540 | |
| 89 | Phosphorylation | GLGAKVHTFVVDCSN CCCCEEEEEEEECCC | 22.55 | 28348404 | |
| 95 | Phosphorylation | HTFVVDCSNREDIYS EEEEEECCCCHHHHH | 34.16 | 28348404 | |
| 101 | Phosphorylation | CSNREDIYSSAKKVK CCCCHHHHHHCHHHH | 14.64 | 28348404 | |
| 102 | Phosphorylation | SNREDIYSSAKKVKA CCCHHHHHHCHHHHC | 24.93 | 28348404 | |
| 103 | Phosphorylation | NREDIYSSAKKVKAE CCHHHHHHCHHHHCE | 27.43 | 28348404 | |
| 105 | 2-Hydroxyisobutyrylation | EDIYSSAKKVKAEIG HHHHHHCHHHHCEEC | 61.11 | - | |
| 105 | Ubiquitination | EDIYSSAKKVKAEIG HHHHHHCHHHHCEEC | 61.11 | 27667366 | |
| 106 | Ubiquitination | DIYSSAKKVKAEIGD HHHHHCHHHHCEECC | 49.00 | 22817900 | |
| 108 | Ubiquitination | YSSAKKVKAEIGDVS HHHCHHHHCEECCEE | 49.54 | 22817900 | |
| 188 | Phosphorylation | FLLAYCSSKFAAVGF HHHHHHCCCCHHCCC | 28.38 | - | |
| 227 | Ubiquitination | FVNTGFIKNPSTSLG CCCCCCCCCCCCCCC | 61.62 | 29967540 | |
| 230 | Phosphorylation | TGFIKNPSTSLGPTL CCCCCCCCCCCCCCC | 39.77 | 27050516 | |
| 232 | Phosphorylation | FIKNPSTSLGPTLEP CCCCCCCCCCCCCCH | 35.35 | 27050516 |
| 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 DHB11_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHB11_HUMAN !! | ||||||
* 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 DHB11_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DHB11_HUMAN !! | ||||
| 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. | ||||||
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