| UniProt ID | CF120_HUMAN | |
|---|---|---|
| UniProt AC | Q7Z4R8 | |
| Protein Name | UPF0669 protein C6orf120 | |
| Gene Name | C6orf120 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 191 | |
| Subcellular Localization | Secreted . Secreted by hepatocytes. | |
| Protein Description | May be involved in induction of apoptosis in CD4(+) T-cells, but not CD8(+) T-cells or hepatocytes.. | |
| Protein Sequence | MAAPRGRAAPWTTALLLLLASQVLSPGSCADEEEVPEEWVLLHVVQGQIGAGNYSYLRLNHEGKIVLRMRSLKGDADLYVSASSLHPSFDDYELQSATCGPDAVSIPAHFRRPVGIGVYGHPSHLESEFEMKVYYDGTVEQHPFGEAAYPADGADAGQKHAGAPEDASQEEESVLWTILISILKLVLEILF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 53 | N-linked_Glycosylation | QGQIGAGNYSYLRLN ECCCCCCCCCEEEEC | 23.26 | 19159218 | |
| 64 | Ubiquitination | LRLNHEGKIVLRMRS EEECCCCEEEEEEEC | 27.02 | - | |
| 72 | N-linked_Glycosylation | IVLRMRSLKGDADLY EEEEEECCCCCCCEE | 5.19 | 19159218 | |
| 98 | O-linked_Glycosylation | DYELQSATCGPDAVS CHHHCCCCCCCCCCC | 24.20 | OGP | |
| 127 | Phosphorylation | GHPSHLESEFEMKVY CCHHHCCCCEEEEEE | 54.68 | - | |
| 138 | O-linked_Glycosylation | MKVYYDGTVEQHPFG EEEEECCCEEECCCC | 20.26 | OGP | |
| 146 | Phosphorylation | VEQHPFGEAAYPADG EEECCCCCCCCCCCC | 30.42 | - | |
| 181 | Phosphorylation | VLWTILISILKLVLE HHHHHHHHHHHHHHH | 20.58 | 24719451 |
| 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 CF120_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CF120_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 CF120_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CF120_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. | ||||||
loading...
| 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-53, AND MASS SPECTROMETRY. | |