| UniProt ID | OIT3_HUMAN | |
|---|---|---|
| UniProt AC | Q8WWZ8 | |
| Protein Name | Oncoprotein-induced transcript 3 protein | |
| Gene Name | OIT3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 545 | |
| Subcellular Localization | Nucleus envelope . Can be secreted into blood. | |
| Protein Description | May be involved in hepatocellular function and development.. | |
| Protein Sequence | MPPFLLLTCLFITGTSVSPVALDPCSAYISLNEPWRNTDHQLDESQGPPLCDNHVNGEWYHFTGMAGDAMPTFCIPENHCGTHAPVWLNGSHPLEGDGIVQRQACASFNGNCCLWNTTVEVKACPGGYYVYRLTKPSVCFHVYCGHFYDICDEDCHGSCSDTSECTCAPGTVLGPDRQTCFDENECEQNNGGCSEICVNLKNSYRCECGVGRVLRSDGKTCEDVEGCHNNNGGCSHSCLGSEKGYQCECPRGLVLSEDNHTCQVPVLCKSNAIEVNIPRELVGGLELFLTNTSCRGVSNGTHVNILFSLKTCGTVVDVVNDKIVASNLVTGLPKQTPGSSGDFIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNSPLEIMSRNHGIFPFTLEIFKDNEFEEPYREALPTLKLRDSLYFGIEPVVHVSGLESLVESCFATPTSKIDEVLKYYLIRDGCVSDDSVKQYTSRDHLAKHFQVPVFKFVGKDHKEVFLHCRVLVCGVLDERSRCAQGCHRRMRRGAGGEDSAGLQGQTLTGGPIRIDWED | |
| 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 |
|---|---|---|---|---|---|
| 89 | N-linked_Glycosylation | THAPVWLNGSHPLEG CCCCEEECCCCCCCC | 33.92 | UniProtKB CARBOHYD | |
| 116 | N-linked_Glycosylation | NGNCCLWNTTVEVKA CCCEEEEEEEEEEEE | 16.96 | UniProtKB CARBOHYD | |
| 131 | Phosphorylation | CPGGYYVYRLTKPSV CCCCEEEEEECCCEE | 5.47 | 22817900 | |
| 220 | Phosphorylation | VLRSDGKTCEDVEGC EECCCCCEECCCCCC | 27.02 | - | |
| 237 | Phosphorylation | NNGGCSHSCLGSEKG CCCCCCCCCCCCCCC | 8.51 | - | |
| 241 | Phosphorylation | CSHSCLGSEKGYQCE CCCCCCCCCCCEECC | 24.16 | - | |
| 245 | Phosphorylation | CLGSEKGYQCECPRG CCCCCCCEECCCCCC | 22.51 | - | |
| 291 | N-linked_Glycosylation | GLELFLTNTSCRGVS CEEEEEECCCCCCCC | 31.94 | 19159218 | |
| 299 | N-linked_Glycosylation | TSCRGVSNGTHVNIL CCCCCCCCCCEEEEE | 57.91 | UniProtKB CARBOHYD | |
| 301 | Phosphorylation | CRGVSNGTHVNILFS CCCCCCCCEEEEEEE | 27.22 | - | |
| 308 | Phosphorylation | THVNILFSLKTCGTV CEEEEEEEECCCCCE | 26.05 | 24719451 | |
| 326 | Phosphorylation | VNDKIVASNLVTGLP HCCEEEHHHHCCCCC | 21.58 | 29396449 | |
| 330 | Phosphorylation | IVASNLVTGLPKQTP EEHHHHCCCCCCCCC | 35.85 | 29396449 | |
| 415 | Phosphorylation | PTLKLRDSLYFGIEP CCCCCCCCEECCCEE | 20.66 | 22210691 | |
| 439 | Phosphorylation | LVESCFATPTSKIDE HHHHHCCCCCHHHHH | 13.57 | 22210691 | |
| 442 | Phosphorylation | SCFATPTSKIDEVLK HHCCCCCHHHHHHHH | 28.90 | 22210691 | |
| 526 | Phosphorylation | RGAGGEDSAGLQGQT CCCCCCCCCCCCCCC | 21.67 | - | |
| 533 | Phosphorylation | SAGLQGQTLTGGPIR CCCCCCCCCCCCCEE | 32.86 | - |
| 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 OIT3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OIT3_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 OIT3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of OIT3_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-291, AND MASSSPECTROMETRY. | |