| UniProt ID | EPDR1_HUMAN | |
|---|---|---|
| UniProt AC | Q9UM22 | |
| Protein Name | Mammalian ependymin-related protein 1 | |
| Gene Name | EPDR1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 224 | |
| Subcellular Localization | Secreted. | |
| Protein Description | ||
| Protein Sequence | MPGRAPLRTVPGALGAWLLGGLWAWTLCGLCSLGAVGAPRPCQAPQQWEGRQVMYQQSSGRNSRALLSYDGLNQRVRVLDERKALIPCKRLFEYILLYKDGVMFQIDQATKQCSKMTLTQPWDPLDIPQNSTFEDQYSIGGPQEQITVQEWSDRKSARSYETWIGIYTVKDCYPVQETFTINYSVILSTRFFDIQLGIKDPSVFTPPSTCQMAQLEKMSEDCSW | |
| 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 |
|---|---|---|---|---|---|
| 103 | Sulfoxidation | LLYKDGVMFQIDQAT HHCCCCEEEEEEHHH | 2.21 | 21406390 | |
| 130 | N-linked_Glycosylation | DPLDIPQNSTFEDQY CCCCCCCCCCCCCCC | 37.35 | 30729188 | |
| 173 | Phosphorylation | IYTVKDCYPVQETFT EEEECCCEECCEEEE | 19.30 | 23607784 | |
| 178 | Phosphorylation | DCYPVQETFTINYSV CCEECCEEEEEEEEE | 14.69 | 23607784 | |
| 180 | O-linked_Glycosylation | YPVQETFTINYSVIL EECCEEEEEEEEEEE | 18.74 | 28657654 | |
| 180 | Phosphorylation | YPVQETFTINYSVIL EECCEEEEEEEEEEE | 18.74 | 23607784 | |
| 182 | N-linked_Glycosylation | VQETFTINYSVILST CCEEEEEEEEEEEEE | 21.70 | UniProtKB CARBOHYD | |
| 183 | Phosphorylation | QETFTINYSVILSTR CEEEEEEEEEEEEEC | 10.64 | 23607784 | |
| 184 | O-linked_Glycosylation | ETFTINYSVILSTRF EEEEEEEEEEEEECE | 9.74 | 28657654 | |
| 184 | Phosphorylation | ETFTINYSVILSTRF EEEEEEEEEEEEECE | 9.74 | 23607784 | |
| 188 | Phosphorylation | INYSVILSTRFFDIQ EEEEEEEEECEEEEE | 13.35 | 23607784 | |
| 189 | Phosphorylation | NYSVILSTRFFDIQL EEEEEEEECEEEEEE | 28.22 | 23607784 |
| 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 EPDR1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EPDR1_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 EPDR1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of EPDR1_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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, AND MASSSPECTROMETRY. | |
