| UniProt ID | DERL2_HUMAN | |
|---|---|---|
| UniProt AC | Q9GZP9 | |
| Protein Name | Derlin-2 {ECO:0000303|PubMed:15215855} | |
| Gene Name | DERL2 {ECO:0000312|HGNC:HGNC:17943} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 239 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. [PubMed: 16186509] | |
| Protein Sequence | MAYQSLRLEYLQIPPVSRAYTTACVLTTAAVQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDVFPNQPGGIRILKTPSILKAIFDTPDEDPNYNPLPEERPGGFAWGEGQRLGG | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MAYQSLRLEY -----CCCCCHHCHH | 9.42 | 27732954 | |
| 5 | Phosphorylation | ---MAYQSLRLEYLQ ---CCCCCHHCHHCC | 11.63 | 27732954 | |
| 17 | Phosphorylation | YLQIPPVSRAYTTAC HCCCCCCCHHHHHHH | 19.57 | 27732954 | |
| 89 | Phosphorylation | CRMLEEGSFRGRTAD HHHHHHCCCCCCCHH | 18.30 | 24719451 | |
| 200 | Ubiquitination | PGGIRILKTPSILKA CCCEEEECCHHHHHH | 56.89 | - | |
| 203 | Phosphorylation | IRILKTPSILKAIFD EEEECCHHHHHHHHC | 45.87 | 24719451 | |
| 206 | Ubiquitination | LKTPSILKAIFDTPD ECCHHHHHHHHCCCC | 37.45 | 21906983 | |
| 211 | Phosphorylation | ILKAIFDTPDEDPNY HHHHHHCCCCCCCCC | 23.14 | - | |
| 218 | Phosphorylation | TPDEDPNYNPLPEER CCCCCCCCCCCCCCC | 24.44 | 28796482 |
| 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 DERL2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DERL2_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 DERL2_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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