| UniProt ID | TSG6_HUMAN | |
|---|---|---|
| UniProt AC | P98066 | |
| Protein Name | Tumor necrosis factor-inducible gene 6 protein | |
| Gene Name | TNFAIP6 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 277 | |
| Subcellular Localization | ||
| Protein Description | Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis.. | |
| Protein Sequence | MIILIYLFLLLWEDTQGWGFKDGIFHNSIWLERAAGVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKQIFKSPGFPNEYEDNQICYWHIRLKYGQRIHLSFLDFDLEDDPGCLADYVEIYDSYDDVHGFVGRYCGDELPDDIISTGNVMTLKFLSDASVTAGGFQIKYVAMDPVSKSSQGKNTSTTSTGNKNFLAGRFSHL | |
| 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 |
|---|---|---|---|---|---|
| 38 | Phosphorylation | LERAAGVYHREARSG HHHHCCCEEHHHHCC | 8.34 | 24719451 | |
| 118 | N-linked_Glycosylation | IDYGIRLNRSERWDA EECEEECCCHHCCEE | 35.27 | UniProtKB CARBOHYD | |
| 148 | Phosphorylation | DPKQIFKSPGFPNEY CHHHHHCCCCCCCCC | 21.36 | - | |
| 155 | Phosphorylation | SPGFPNEYEDNQICY CCCCCCCCCCCCEEE | 34.91 | - | |
| 258 | N-linked_Glycosylation | SKSSQGKNTSTTSTG CCCCCCCCCCCCCCC | 46.19 | UniProtKB CARBOHYD | |
| 259 | Phosphorylation | KSSQGKNTSTTSTGN CCCCCCCCCCCCCCC | 30.82 | 22817900 | |
| 262 | Phosphorylation | QGKNTSTTSTGNKNF CCCCCCCCCCCCCCE | 24.86 | 22817900 |
| 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 TSG6_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSG6_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|
| 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 |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND THR-262, ANDMASS SPECTROMETRY. | |