| UniProt ID | DHB7_HUMAN | |
|---|---|---|
| UniProt AC | P56937 | |
| Protein Name | 3-keto-steroid reductase | |
| Gene Name | HSD17B7 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 341 | |
| Subcellular Localization |
Cell membrane Single-pass membrane protein. |
|
| Protein Description | Responsible for the reduction of the keto group on the C-3 of sterols.. | |
| Protein Sequence | MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFSLEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIWTLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQKMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL | |
| 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 |
|---|---|---|---|---|---|
| 37 | N-linked_Glycosylation | HLCLACRNMSKAEAV HHHHHCCCCCHHHHH | 38.68 | UniProtKB CARBOHYD | |
| 118 | Phosphorylation | RKVIHMFSTAEGLLT HHHHHHHHCCCCCCC | 21.09 | - | |
| 125 | Phosphorylation | STAEGLLTQGDKITA HCCCCCCCCCCEEEH | 35.23 | - | |
| 168 (in isoform 2) | Ubiquitination | - | 9.98 | 21890473 | |
| 176 (in isoform 1) | Ubiquitination | - | 49.85 | 21890473 | |
| 176 (in isoform 3) | Ubiquitination | - | 49.85 | 21890473 | |
| 176 | Ubiquitination | TSSRSARKSNFSLED ECCCCCCCCCCCHHH | 49.85 | 21906983 | |
| 177 | Phosphorylation | SSRSARKSNFSLEDF CCCCCCCCCCCHHHH | 37.24 | 30108239 | |
| 178 | N-linked_Glycosylation | SRSARKSNFSLEDFQ CCCCCCCCCCHHHHC | 33.29 | UniProtKB CARBOHYD | |
| 180 (in isoform 2) | Ubiquitination | - | 34.79 | 21890473 | |
| 180 | Phosphorylation | SARKSNFSLEDFQHS CCCCCCCCHHHHCCC | 34.79 | 30108239 | |
| 187 | Phosphorylation | SLEDFQHSKGKEPYS CHHHHCCCCCCCCCC | 32.11 | 23927012 | |
| 188 (in isoform 1) | Ubiquitination | - | 72.39 | 21890473 | |
| 188 (in isoform 3) | Ubiquitination | - | 72.39 | 21890473 | |
| 188 | Ubiquitination | LEDFQHSKGKEPYSS HHHHCCCCCCCCCCC | 72.39 | 21906983 | |
| 190 | Ubiquitination | DFQHSKGKEPYSSSK HHCCCCCCCCCCCCH | 60.29 | - | |
| 197 | Ubiquitination | KEPYSSSKYATDLLS CCCCCCCHHHHHHHH | 40.63 | - | |
| 198 | Phosphorylation | EPYSSSKYATDLLSV CCCCCCHHHHHHHHH | 19.38 | - | |
| 229 | N-linked_Glycosylation | CPGTALTNLTYGILP CCCHHHHHCCCCCCH | 31.10 | UniProtKB CARBOHYD | |
| 266 (in isoform 3) | Ubiquitination | - | 41.21 | 21890473 | |
| 276 (in isoform 3) | Ubiquitination | - | 29.82 | 21890473 | |
| 280 (in isoform 3) | Ubiquitination | - | 38.31 | 21890473 | |
| 287 | Phosphorylation | NPLIKYLSATTGFGR CHHHHHHHCCCCCCC | 22.08 | 22210691 | |
| 290 | Phosphorylation | IKYLSATTGFGRNYI HHHHHCCCCCCCCCC | 30.17 | 22210691 | |
| 293 (in isoform 2) | Ubiquitination | - | 20.47 | 21890473 | |
| 294 (in isoform 3) | Ubiquitination | - | 30.44 | 21890473 | |
| 301 (in isoform 1) | Ubiquitination | - | 25.80 | 21890473 | |
| 301 | Ubiquitination | RNYIMTQKMDLDEDT CCCCCEECCCCCHHH | 25.80 | 21906983 | |
| 303 (in isoform 2) | Ubiquitination | - | 58.99 | 21890473 | |
| 307 (in isoform 2) | Ubiquitination | - | 51.38 | 21890473 | |
| 311 (in isoform 1) | Ubiquitination | - | 47.08 | 21890473 | |
| 311 | Ubiquitination | LDEDTAEKFYQKLLE CCHHHHHHHHHHHHH | 47.08 | 21906983 | |
| 313 | Phosphorylation | EDTAEKFYQKLLELE HHHHHHHHHHHHHHH | 18.79 | 29496907 | |
| 315 (in isoform 1) | Ubiquitination | - | 43.59 | 21890473 | |
| 315 | Ubiquitination | TAEKFYQKLLELEKH HHHHHHHHHHHHHHH | 43.59 | 21890473 | |
| 321 (in isoform 2) | Ubiquitination | - | 57.89 | 21890473 | |
| 321 | Ubiquitination | QKLLELEKHIRVTIQ HHHHHHHHHHEEEEE | 57.89 | 19608861 | |
| 321 | Acetylation | QKLLELEKHIRVTIQ HHHHHHHHHHEEEEE | 57.89 | 19608861 | |
| 329 (in isoform 1) | Ubiquitination | - | 54.73 | 21890473 | |
| 329 | Ubiquitination | HIRVTIQKTDNQARL HHEEEEEECCCCHHH | 54.73 | 2190698 | |
| 337 | Phosphorylation | TDNQARLSGSCL--- CCCCHHHCCCCC--- | 24.09 | 25159151 | |
| 339 | Phosphorylation | NQARLSGSCL----- CCHHHCCCCC----- | 14.63 | 30108239 |
| 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 DHB7_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHB7_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 DHB7_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DPOLB_HUMAN | POLB | physical | 26186194 | |
| SLAF1_HUMAN | SLAMF1 | physical | 26186194 | |
| PPA5_HUMAN | ACP5 | physical | 26186194 | |
| PPA5_HUMAN | ACP5 | physical | 28514442 | |
| DPOLB_HUMAN | POLB | physical | 28514442 | |
| AAAT_HUMAN | SLC1A5 | physical | 28514442 | |
| SLAF1_HUMAN | SLAMF1 | physical | 28514442 |
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND MASS SPECTROMETRY. | |
