| UniProt ID | TNR14_HUMAN | |
|---|---|---|
| UniProt AC | Q92956 | |
| Protein Name | Tumor necrosis factor receptor superfamily member 14 | |
| Gene Name | TNFRSF14 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 283 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
| Protein Description | Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells.; (Microbial infection) Acts as a receptor for Herpes simplex virus 1/HHV-1.; (Microbial infection) Acts as a receptor for Herpes simplex virus 2/HHV-2.. | |
| Protein Sequence | MEPPGDWGPPPWRSTPKTDVLRLVLYLTFLGAPCYAPALPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLNGLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAACRAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWLVTKAGAGTSSSHWVWWFLSGSLVIVIVCSTVGLIICVKRRKPRGDVVKVIVSVQRKRQEAEGEATVIEALQAPPDVTTVAVEETIPSFTGRSPNH | |
| 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 |
|---|---|---|---|---|---|
| 16 (in isoform 2) | Phosphorylation | - | 38.50 | 16964243 | |
| 110 | N-linked_Glycosylation | MGLRASRNCSRTENA HCHHHHCCCCCCCCC | 26.14 | 16169851 | |
| 141 | Phosphorylation | HCAACRAYATSSPGQ CEEECHHEECCCCCC | 7.34 | 19413330 | |
| 173 | N-linked_Glycosylation | PPGTFSPNGTLEECQ CCCCCCCCCCHHHHH | 55.68 | UniProtKB CARBOHYD | |
| 240 | Phosphorylation | DVVKVIVSVQRKRQE CEEEEEEEEHHHHHH | 11.04 | 23401153 |
| 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 TNR14_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TNR14_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 TNR14_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| UGGG1_HUMAN | UGGT1 | physical | 17353931 | |
| GCN1_HUMAN | GCN1L1 | physical | 17353931 | |
| PDIA1_HUMAN | P4HB | physical | 17353931 | |
| SC11A_HUMAN | SEC11A | physical | 17353931 | |
| PDIA6_HUMAN | PDIA6 | physical | 17353931 | |
| CHD3_HUMAN | CHD3 | physical | 16169070 | |
| VIME_HUMAN | VIM | physical | 16169070 | |
| TRAF5_HUMAN | TRAF5 | physical | 9153189 | |
| TRAF2_HUMAN | TRAF2 | physical | 9153189 | |
| TRAF5_HUMAN | TRAF5 | physical | 9162022 | |
| TRAF3_HUMAN | TRAF3 | physical | 9162022 | |
| TRAF1_HUMAN | TRAF1 | physical | 9162022 | |
| TRAF2_HUMAN | TRAF2 | physical | 9162022 | |
| TZAP_HUMAN | ZBTB48 | physical | 21900206 | |
| UBQL4_HUMAN | UBQLN4 | physical | 21900206 | |
| TIP_HUMAN | ITFG1 | physical | 21900206 | |
| NC2A_HUMAN | DRAP1 | physical | 21900206 | |
| DYL1_HUMAN | DYNLL1 | physical | 21900206 | |
| WDR73_HUMAN | WDR73 | physical | 21900206 | |
| KAIN_HUMAN | SERPINA4 | physical | 21900206 | |
| A2MG_HUMAN | A2M | physical | 21900206 | |
| DGKD_HUMAN | DGKD | physical | 21900206 | |
| CE126_HUMAN | KIAA1377 | physical | 21900206 | |
| MBTP1_HUMAN | MBTPS1 | physical | 21900206 | |
| NDUS2_HUMAN | NDUFS2 | physical | 21900206 | |
| IMPA2_HUMAN | IMPA2 | physical | 21900206 | |
| A4_HUMAN | APP | physical | 21832049 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| N-linked Glycosylation | |
| Reference | PubMed |
| "Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex."; Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D.,Hymowitz S.G.; J. Biol. Chem. 280:39553-39561(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH BTLA,AND GLYCOSYLATION AT ASN-110. | |
| Phosphorylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND MASSSPECTROMETRY. | |
