| UniProt ID | RCN3_HUMAN | |
|---|---|---|
| UniProt AC | Q96D15 | |
| Protein Name | Reticulocalbin-3 | |
| Gene Name | RCN3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 328 | |
| Subcellular Localization | Endoplasmic reticulum lumen . | |
| Protein Description | ||
| Protein Sequence | MMWRPSVLLLLLLLRHGAQGKPSPDAGPHGQGRVHQAAPLSDAPHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVGSQATNYGEDLTRHHDEL | |
| 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 |
|---|---|---|---|---|---|
| 54 | Phosphorylation | DAHGNFQYDHEAFLG CCCCCCCCCHHHHHC | 18.35 | - | |
| 66 | Ubiquitination | FLGREVAKEFDQLTP HHCHHHHHHHHHCCH | 65.18 | 23000965 | |
| 117 | Phosphorylation | QQRHIRDSVSAAWDT HHHHHHHHHHHHHHC | 14.23 | 27251275 | |
| 140 | N-linked_Glycosylation | VGWEELRNATYGHYA CCHHHHHHCCCCCCC | 49.62 | 19159218 | |
| 142 | O-linked_Glycosylation | WEELRNATYGHYAPG HHHHHHCCCCCCCCC | 33.32 | 30059200 | |
| 181 | Phosphorylation | VADQDGDSMATREEL EECCCCCCCCCHHHH | 18.82 | 21406692 | |
| 184 | Phosphorylation | QDGDSMATREELTAF CCCCCCCCHHHHHHH | 29.94 | 21406692 | |
| 200 | Sulfoxidation | HPEEFPHMRDIVIAE CHHHCCCHHHHEEEC | 4.13 | 30846556 | |
| 308 | Sulfoxidation | EILGNWNMFVGSQAT HHCCCCHHEECHHHC | 1.86 | 30846556 |
| 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 RCN3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RCN3_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 RCN3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PRUN2_HUMAN | PRUNE2 | physical | 16189514 | |
| HID1_HUMAN | HID1 | physical | 16189514 | |
| KLH42_HUMAN | KLHL42 | physical | 16189514 | |
| STAT6_HUMAN | STAT6 | physical | 21988832 | |
| PACRL_HUMAN | PACRGL | physical | 25416956 |
| 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-140, AND MASSSPECTROMETRY. | |