| UniProt ID | DERL1_HUMAN | |
|---|---|---|
| UniProt AC | Q9BUN8 | |
| Protein Name | Derlin-1 {ECO:0000303|PubMed:15215855} | |
| Gene Name | DERL1 {ECO:0000312|HGNC:HGNC:28454} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 251 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. [PubMed: 15215856 Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation] | |
| Protein Sequence | MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ | |
| 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 | ------MSDIGDWFR ------CCCHHHHHH | 37.62 | 22223895 | |
| 190 | Phosphorylation | YFFLMFRYPMDLGGR HHHHHHCCCCCCCCC | 7.52 | - | |
| 201 | Phosphorylation | LGGRNFLSTPQFLYR CCCCCCCCCHHHHHH | 33.63 | 20058876 | |
| 202 | Phosphorylation | GGRNFLSTPQFLYRW CCCCCCCCHHHHHHH | 24.21 | 21712546 | |
| 207 | Phosphorylation | LSTPQFLYRWLPSRR CCCHHHHHHHCCCCC | 10.88 | 27251275 | |
| 214 | Methylation | YRWLPSRRGGVSGFG HHHCCCCCCCCCCCC | 51.02 | - | |
| 218 | Phosphorylation | PSRRGGVSGFGVPPA CCCCCCCCCCCCCCH | 31.51 | - | |
| 226 | Phosphorylation | GFGVPPASMRRAADQ CCCCCCHHHCCHHHH | 20.70 | 23401153 | |
| 227 | Sulfoxidation | FGVPPASMRRAADQN CCCCCHHHCCHHHHC | 3.50 | 21406390 |
| 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 DERL1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DERL1_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 DERL1_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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| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202, AND MASSSPECTROMETRY. | |
