| UniProt ID | TNR6_HUMAN | |
|---|---|---|
| UniProt AC | P25445 | |
| Protein Name | Tumor necrosis factor receptor superfamily member 6 | |
| Gene Name | FAS | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 335 | |
| Subcellular Localization |
Isoform 1: Cell membrane Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Secreted. Isoform 6: Secreted. |
|
| Protein Description | Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro).. | |
| Protein Sequence | MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV | |
| 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 |
|---|---|---|---|---|---|
| 28 | O-linked_Glycosylation | KSVNAQVTDINSKGL CCCCCEEECCHHHCC | 21.05 | 22171320 | |
| 33 | Ubiquitination | QVTDINSKGLELRKT EEECCHHHCCEEEEE | 64.13 | - | |
| 40 | O-linked_Glycosylation | KGLELRKTVTTVETQ HCCEEEEEEEEEEEC | 19.36 | 55827405 | |
| 42 | O-linked_Glycosylation | LELRKTVTTVETQNL CEEEEEEEEEEECCC | 30.29 | 55827409 | |
| 43 | O-linked_Glycosylation | ELRKTVTTVETQNLE EEEEEEEEEEECCCC | 16.41 | 55827413 | |
| 46 | O-linked_Glycosylation | KTVTTVETQNLEGLH EEEEEEEECCCCCCC | 20.58 | 55827417 | |
| 91 | Phosphorylation | PCQEGKEYTDKAHFS ECCCCCCCCCHHHHC | 24.59 | 15660394 | |
| 118 | N-linked_Glycosylation | HGLEVEINCTRTQNT CCEEEEEEEECCCCC | 13.96 | 19159218 | |
| 120 | Phosphorylation | LEVEINCTRTQNTKC EEEEEEEECCCCCCC | 32.06 | 24505115 | |
| 136 | N-linked_Glycosylation | CKPNFFCNSTVCEHC ECCCEEECCCCCCCC | 35.24 | UniProtKB CARBOHYD | |
| 198 | Phosphorylation | KRKEVQKTCRKHRKE CHHHHHHHHHHHHHH | 10.64 | 18669648 | |
| 199 | S-palmitoylation | RKEVQKTCRKHRKEN HHHHHHHHHHHHHHH | 7.60 | 25301068 | |
| 204 | Ubiquitination | KTCRKHRKENQGSHE HHHHHHHHHHCCCCC | 61.82 | - | |
| 209 | Phosphorylation | HRKENQGSHESPTLN HHHHHCCCCCCCCCC | 17.83 | 30266825 | |
| 212 | Phosphorylation | ENQGSHESPTLNPET HHCCCCCCCCCCCCE | 20.12 | 30266825 | |
| 214 | Phosphorylation | QGSHESPTLNPETVA CCCCCCCCCCCCEEE | 48.74 | 30266825 | |
| 214 | O-linked_Glycosylation | QGSHESPTLNPETVA CCCCCCCCCCCCEEE | 48.74 | OGP | |
| 219 | Phosphorylation | SPTLNPETVAINLSD CCCCCCCEEEEECHH | 19.25 | 30278072 | |
| 219 | O-linked_Glycosylation | SPTLNPETVAINLSD CCCCCCCEEEEECHH | 19.25 | OGP | |
| 225 | Phosphorylation | ETVAINLSDVDLSKY CEEEEECHHCCHHHH | 30.97 | 7540117 | |
| 230 | Phosphorylation | NLSDVDLSKYITTIA ECHHCCHHHHHHHHH | 20.96 | 23927012 | |
| 232 | Phosphorylation | SDVDLSKYITTIAGV HHCCHHHHHHHHHHH | 10.50 | 29978859 | |
| 234 | Phosphorylation | VDLSKYITTIAGVMT CCHHHHHHHHHHHHH | 14.73 | 29978859 | |
| 235 | Phosphorylation | DLSKYITTIAGVMTL CHHHHHHHHHHHHHH | 10.16 | 20049867 | |
| 241 | Phosphorylation | TTIAGVMTLSQVKGF HHHHHHHHHHHHHHH | 22.35 | 30108239 | |
| 242 (in isoform 6) | Ubiquitination | - | 1.49 | 21906983 | |
| 243 | Phosphorylation | IAGVMTLSQVKGFVR HHHHHHHHHHHHHHH | 24.62 | 30108239 | |
| 263 (in isoform 1) | Ubiquitination | - | 57.09 | 21906983 | |
| 263 | Ubiquitination | EAKIDEIKNDNVQDT HHHHHHHCCCCCCCH | 57.09 | 21906983 | |
| 267 (in isoform 6) | Ubiquitination | - | 6.42 | 21906983 | |
| 270 | Phosphorylation | KNDNVQDTAEQKVQL CCCCCCCHHHHHHHH | 18.27 | 27174698 | |
| 274 | Ubiquitination | VQDTAEQKVQLLRNW CCCHHHHHHHHHHHH | 24.37 | - | |
| 287 | Ubiquitination | NWHQLHGKKEAYDTL HHHHHCCCHHHHHHH | 36.37 | - | |
| 287 | 2-Hydroxyisobutyrylation | NWHQLHGKKEAYDTL HHHHHCCCHHHHHHH | 36.37 | - | |
| 288 (in isoform 1) | Ubiquitination | - | 52.77 | 21906983 | |
| 288 | Ubiquitination | WHQLHGKKEAYDTLI HHHHCCCHHHHHHHH | 52.77 | 21906983 | |
| 291 | Phosphorylation | LHGKKEAYDTLIKDL HCCCHHHHHHHHHHH | 15.56 | 16187021 | |
| 293 | Phosphorylation | GKKEAYDTLIKDLKK CCHHHHHHHHHHHHH | 20.08 | 28355574 | |
| 295 (in isoform 6) | Ubiquitination | - | 3.37 | 21906983 | |
| 296 | Ubiquitination | EAYDTLIKDLKKANL HHHHHHHHHHHHCCC | 61.18 | - | |
| 299 | Acetylation | DTLIKDLKKANLCTL HHHHHHHHHCCCHHH | 61.03 | 25953088 | |
| 299 | Malonylation | DTLIKDLKKANLCTL HHHHHHHHHCCCHHH | 61.03 | 26320211 | |
| 300 | Malonylation | TLIKDLKKANLCTLA HHHHHHHHCCCHHHH | 50.21 | 26320211 | |
| 300 | Ubiquitination | TLIKDLKKANLCTLA HHHHHHHHCCCHHHH | 50.21 | - | |
| 305 | Phosphorylation | LKKANLCTLAEKIQT HHHCCCHHHHHHHHH | 31.97 | 30108239 | |
| 309 | Ubiquitination | NLCTLAEKIQTIILK CCHHHHHHHHHHHHH | 34.21 | - | |
| 312 | Phosphorylation | TLAEKIQTIILKDIT HHHHHHHHHHHHHCC | 17.29 | 23312004 | |
| 316 | Ubiquitination | KIQTIILKDITSDSE HHHHHHHHHCCCCCC | 36.35 | 2190698 | |
| 316 (in isoform 1) | Ubiquitination | - | 36.35 | 21906983 | |
| 320 | Phosphorylation | IILKDITSDSENSNF HHHHHCCCCCCCCCH | 39.20 | 28674419 | |
| 322 | Phosphorylation | LKDITSDSENSNFRN HHHCCCCCCCCCHHH | 38.14 | 28674419 | |
| 325 | Phosphorylation | ITSDSENSNFRNEIQ CCCCCCCCCHHHHHH | 33.04 | 26437602 | |
| 333 | Phosphorylation | NFRNEIQSLV----- CHHHHHHHCC----- | 36.44 | 30108239 |
| 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 TNR6_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TNR6_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 TNR6_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00005 | Chronic lymphocytic leukemia (CLL) | |||||
| H00007 | Hodgkin lymphoma | |||||
| H00009 | Adult T-cell leukemia | |||||
| H00017 | Esophageal cancer | |||||
| OMIM Disease | ||||||
| 601859 | Autoimmune lymphoproliferative syndrome 1A (ALPS1A) | |||||
| 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-118, AND MASSSPECTROMETRY. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-28, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND THR-214, ANDMASS SPECTROMETRY. | |
